Crystal Structure of Human BPI and Two Bound Phospholipids at 2.4 Angstrom Resolution

Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial protein of 456 residues, binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria. At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule f...

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Published in:Science (American Association for the Advancement of Science) 1997-06, Vol.276 (5320), p.1861-1864
Main Authors: Beamer, Lesa J., Carroll, Stephen F., Eisenberg, David
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Antibacterial agents
Antimicrobial Cationic Peptides
Atoms
Bacteria
Binding and carrier proteins
Binding Sites
Biological and medical sciences
Blood Bactericidal Activity
Blood Proteins - chemistry
Blood Proteins - metabolism
Crystal structure
Crystallization
Crystallography, X-Ray
Crystals
Datasets
Disulfides
Electron density
Endotoxins
Fundamental and applied biological sciences. Psychology
Humans
Infections
Lipids
Lipopolysaccharides - metabolism
Medical research
Membrane Proteins
Models, Molecular
Molecular Sequence Data
Molecules
Phosphatidylcholines - chemistry
Phosphatidylcholines - metabolism
Phospholipids
Physiological aspects
Protein Conformation
Protein structure
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Scientific Concepts
Structural Elements (Construction)
Structure
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cited_by cdi_FETCH-LOGICAL-c749t-3c16937077ec06cd465c20bda2f56be9f7c85a2ac1a155f54be3835eec71ab553
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container_issue 5320
container_start_page 1861
container_title Science (American Association for the Advancement of Science)
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creator Beamer, Lesa J.
Carroll, Stephen F.
Eisenberg, David
description Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial protein of 456 residues, binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria. At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule formed by two similar domains. Two apolar pockets on the concave surface of the boomerang each bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. As a model for the related plasma lipid transfer proteins, BPI illuminates a mechanism of lipid transfer for this protein family.
doi_str_mv 10.1126/science.276.5320.1861
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At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule formed by two similar domains. Two apolar pockets on the concave surface of the boomerang each bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. 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Psychology ; Humans ; Infections ; Lipids ; Lipopolysaccharides - metabolism ; Medical research ; Membrane Proteins ; Models, Molecular ; Molecular Sequence Data ; Molecules ; Phosphatidylcholines - chemistry ; Phosphatidylcholines - metabolism ; Phospholipids ; Physiological aspects ; Protein Conformation ; Protein structure ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins ; Scientific Concepts ; Structural Elements (Construction) ; Structure</subject><ispartof>Science (American Association for the Advancement of Science), 1997-06, Vol.276 (5320), p.1861-1864</ispartof><rights>Copyright 1997 American Association for the Advancement of Science</rights><rights>1997 INIST-CNRS</rights><rights>COPYRIGHT 1997 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1997 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Jun 20, 1997</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c749t-3c16937077ec06cd465c20bda2f56be9f7c85a2ac1a155f54be3835eec71ab553</citedby><cites>FETCH-LOGICAL-c749t-3c16937077ec06cd465c20bda2f56be9f7c85a2ac1a155f54be3835eec71ab553</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/213572029/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$H</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/213572029?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,780,784,2884,2885,21378,21394,27924,27925,33611,33612,33877,33878,43733,43880,74093,74269</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=2718029$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9188532$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Beamer, Lesa J.</creatorcontrib><creatorcontrib>Carroll, Stephen F.</creatorcontrib><creatorcontrib>Eisenberg, David</creatorcontrib><title>Crystal Structure of Human BPI and Two Bound Phospholipids at 2.4 Angstrom Resolution</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial protein of 456 residues, binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria. At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule formed by two similar domains. Two apolar pockets on the concave surface of the boomerang each bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. As a model for the related plasma lipid transfer proteins, BPI illuminates a mechanism of lipid transfer for this protein family.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Antibacterial agents</subject><subject>Antimicrobial Cationic Peptides</subject><subject>Atoms</subject><subject>Bacteria</subject><subject>Binding and carrier proteins</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Blood Bactericidal Activity</subject><subject>Blood Proteins - chemistry</subject><subject>Blood Proteins - metabolism</subject><subject>Crystal structure</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>Datasets</subject><subject>Disulfides</subject><subject>Electron density</subject><subject>Endotoxins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Infections</subject><subject>Lipids</subject><subject>Lipopolysaccharides - metabolism</subject><subject>Medical research</subject><subject>Membrane Proteins</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Molecules</subject><subject>Phosphatidylcholines - chemistry</subject><subject>Phosphatidylcholines - metabolism</subject><subject>Phospholipids</subject><subject>Physiological aspects</subject><subject>Protein Conformation</subject><subject>Protein structure</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Scientific Concepts</subject><subject>Structural Elements (Construction)</subject><subject>Structure</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>ALSLI</sourceid><sourceid>CJNVE</sourceid><sourceid>M0P</sourceid><recordid>eNqN019v0zAQAPAIgUYZfAMmWQgBD0vxnziOH9sKukoVndjGq-U6ly5VEhfbEezb49JqqKiCKg-JfL8727EvSS4IHhJC84_e1NAZGFKRDzmjcbTIyZNkQLDkqaSYPU0GGLM8LbDgz5MX3q8xjjHJzpIzSYoiJg2Su4l78EE36Ca43oTeAbIVuupb3aHx9QzprkS3Pywa2z5-Xd9bv7m3Tb2pS490QHSYoVG38sHZFn0Fb5s-1LZ7mTyrdOPh1f59ntx9_nQ7uUrni-lsMpqnRmQypMyQXDKBhQCDc1NmOTcUL0tNK54vQVbCFFxTbYgmnFc8WwIrGAcwgugl5-w8eberu3H2ew8-qLb2BppGd2B7r4TEOZaZiPD9v2HGePx9cTX_K0m45Bn_Pfebv-Da9q6L21WUMC4opttqlzu00g2ouqtscNqsoAOnG9tBVcfhEZG8wFKyyNMjPD4ltLU55j8c-EgC_Awr3XuvZjdfTqaLbyfT8fRUWkznB_TyGDW2aWAFKt6LyeKA8x03znrvoFIbV7faPSiC1bYB1L4BVGwAtW0AtW2AmHexP5Z-2UL5mLW_8TH-dh_X3uimcroztX9kVJBid3Cvd2ztg3V_woVkGZHsF2XlEn4</recordid><startdate>19970620</startdate><enddate>19970620</enddate><creator>Beamer, Lesa J.</creator><creator>Carroll, Stephen F.</creator><creator>Eisenberg, David</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>0-V</scope><scope>3V.</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88B</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ALSLI</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CJNVE</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9-</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0K</scope><scope>M0P</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEDU</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>7T5</scope><scope>7X8</scope></search><sort><creationdate>19970620</creationdate><title>Crystal Structure of Human BPI and Two Bound Phospholipids at 2.4 Angstrom Resolution</title><author>Beamer, Lesa J. ; 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At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule formed by two similar domains. Two apolar pockets on the concave surface of the boomerang each bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. As a model for the related plasma lipid transfer proteins, BPI illuminates a mechanism of lipid transfer for this protein family.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>9188532</pmid><doi>10.1126/science.276.5320.1861</doi><tpages>4</tpages></addata></record>
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subjects Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Antibacterial agents
Antimicrobial Cationic Peptides
Atoms
Bacteria
Binding and carrier proteins
Binding Sites
Biological and medical sciences
Blood Bactericidal Activity
Blood Proteins - chemistry
Blood Proteins - metabolism
Crystal structure
Crystallization
Crystallography, X-Ray
Crystals
Datasets
Disulfides
Electron density
Endotoxins
Fundamental and applied biological sciences. Psychology
Humans
Infections
Lipids
Lipopolysaccharides - metabolism
Medical research
Membrane Proteins
Models, Molecular
Molecular Sequence Data
Molecules
Phosphatidylcholines - chemistry
Phosphatidylcholines - metabolism
Phospholipids
Physiological aspects
Protein Conformation
Protein structure
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Scientific Concepts
Structural Elements (Construction)
Structure
title Crystal Structure of Human BPI and Two Bound Phospholipids at 2.4 Angstrom Resolution
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