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D-Glyceraldehyde-3-Phosphate Dehydrogenase: Three-Dimensional Structure and Evolutionary Significance
A 3.0- angstrom resolution electron density map of lobster glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) was computed. The essentially single isomorphous replacement map was very substantially improved by averaging subunits. NAD binds in an open conformation at sites close to subunit interf...
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Published in: | Proceedings of the National Academy of Sciences - PNAS 1973-11, Vol.70 (11), p.3052-3054 |
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container_title | Proceedings of the National Academy of Sciences - PNAS |
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creator | Buehner, Manfred Ford, Geoffrey C. Moras, Dino Olsen, Kenneth W. Rossmann, Michael G. |
description | A 3.0- angstrom resolution electron density map of lobster glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) was computed. The essentially single isomorphous replacement map was very substantially improved by averaging subunits. NAD binds in an open conformation at sites close to subunit interfaces. The coenzyme binding portion of the enzyme has almost the same fold as the corresponding portion of lactate dehydrogenase (EC 1.1.1.27). The presence of this structure in the five enzymes, analyzed so far, that use nucleotide coenzymes might indicate a fundamental primordial structural element. |
doi_str_mv | 10.1073/pnas.70.11.3052 |
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The presence of this structure in the five enzymes, analyzed so far, that use nucleotide coenzymes might indicate a fundamental primordial structural element.</description><subject>Alcohols</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological Evolution</subject><subject>Biological Sciences: Biochemistry</subject><subject>Coenzymes</subject><subject>Dehydrogenases</subject><subject>Dimers</subject><subject>Electron density</subject><subject>Enzymes</subject><subject>Evolution</subject><subject>Genetic Code</subject><subject>Glyceraldehyde-3-Phosphate Dehydrogenases</subject><subject>L-Lactate Dehydrogenase</subject><subject>Lactates</subject><subject>Liver</subject><subject>Models, Structural</subject><subject>NAD</subject><subject>Nephropidae</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>X-Ray Diffraction</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><recordid>eNp9kc1rFDEYxoModa2eBUGZk56yzcdMMiN4kG6tQkGh9RyyyTs7KbPJmmSK-9-bYddVL14S3vf5vR_Jg9BLSpaUSH6x8zotZQnokpOGPUILSjqKRd2Rx2hBCJO4rVn9FD1L6Z4Q0jUtOUNnNRdUSLZAsMLX495A1KOFYW8Bc_xtCGk36AzVak7FsIEyBd5Xd0MEwCu3BZ9c8HqsbnOcTJ4iVNrb6uohjFOelbivbt3Gu94Z7Q08R096PSZ4cbzP0fdPV3eXn_HN1-svlx9vsOFSMMzWPVu3TdMI23LLrdGN7DnUtZwPyxm01gjBNOUNkdTQtZ2TvQHZC64lP0cfDn1303oL1oDP5WFqF922rKSCdupfxbtBbcKDqpks_1Hq3x7rY_gxQcpq65KBcdQewpRUyxihjLcFvDiAJoaUIvSnGZSo2Rg1G6NkCaiajSkVr_9e7cQfnSj6u6M-F_5W_zRQ_TSOGX7mQr75L1mAVwfgPuUQT4RgHe34LxpjrVI</recordid><startdate>19731101</startdate><enddate>19731101</enddate><creator>Buehner, Manfred</creator><creator>Ford, Geoffrey C.</creator><creator>Moras, Dino</creator><creator>Olsen, Kenneth W.</creator><creator>Rossmann, Michael G.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19731101</creationdate><title>D-Glyceraldehyde-3-Phosphate Dehydrogenase: Three-Dimensional Structure and Evolutionary Significance</title><author>Buehner, Manfred ; Ford, Geoffrey C. ; Moras, Dino ; Olsen, Kenneth W. ; Rossmann, Michael G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3762-2bf2b85556d83d3dca57f3e4473e44d32e8dc662a135071c1bdd32efce7f63a73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Alcohols</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biological Evolution</topic><topic>Biological Sciences: Biochemistry</topic><topic>Coenzymes</topic><topic>Dehydrogenases</topic><topic>Dimers</topic><topic>Electron density</topic><topic>Enzymes</topic><topic>Evolution</topic><topic>Genetic Code</topic><topic>Glyceraldehyde-3-Phosphate Dehydrogenases</topic><topic>L-Lactate Dehydrogenase</topic><topic>Lactates</topic><topic>Liver</topic><topic>Models, Structural</topic><topic>NAD</topic><topic>Nephropidae</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Buehner, Manfred</creatorcontrib><creatorcontrib>Ford, Geoffrey C.</creatorcontrib><creatorcontrib>Moras, Dino</creatorcontrib><creatorcontrib>Olsen, Kenneth W.</creatorcontrib><creatorcontrib>Rossmann, Michael G.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Buehner, Manfred</au><au>Ford, Geoffrey C.</au><au>Moras, Dino</au><au>Olsen, Kenneth W.</au><au>Rossmann, Michael G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>D-Glyceraldehyde-3-Phosphate Dehydrogenase: Three-Dimensional Structure and Evolutionary Significance</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1973-11-01</date><risdate>1973</risdate><volume>70</volume><issue>11</issue><spage>3052</spage><epage>3054</epage><pages>3052-3054</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>A 3.0- angstrom resolution electron density map of lobster glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) was computed. The essentially single isomorphous replacement map was very substantially improved by averaging subunits. NAD binds in an open conformation at sites close to subunit interfaces. The coenzyme binding portion of the enzyme has almost the same fold as the corresponding portion of lactate dehydrogenase (EC 1.1.1.27). The presence of this structure in the five enzymes, analyzed so far, that use nucleotide coenzymes might indicate a fundamental primordial structural element.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>4361672</pmid><doi>10.1073/pnas.70.11.3052</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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source | JSTOR Archival Journals and Primary Sources Collection; PubMed Central |
subjects | Alcohols Animals Binding Sites Biological Evolution Biological Sciences: Biochemistry Coenzymes Dehydrogenases Dimers Electron density Enzymes Evolution Genetic Code Glyceraldehyde-3-Phosphate Dehydrogenases L-Lactate Dehydrogenase Lactates Liver Models, Structural NAD Nephropidae Protein Conformation Proteins X-Ray Diffraction |
title | D-Glyceraldehyde-3-Phosphate Dehydrogenase: Three-Dimensional Structure and Evolutionary Significance |
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