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Three‐dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin
The three‐dimensional structure of the fungal serine protease proteinase K has been determined at 3.3 A resolution by single crystal X‐ray diffraction analysis. The enzyme crystallizes in the tetragonal space group P4(3)2(1)2 with cell constants a = b = 68.3 A, c = 108.5 A. The asymmetric unit consi...
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| Published in: | The EMBO journal 1984-06, Vol.3 (6), p.1311-1314 |
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| Main Authors: | , , , , , , , , |
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| container_end_page | 1314 |
| container_issue | 6 |
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| container_title | The EMBO journal |
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| creator | Pähler, A. Banerjee, A. Dattagupta, J.K. Fujiwara, T. Lindner, K. Pal, G.P. Suck, D. Weber, G. Saenger, W. |
| description | The three‐dimensional structure of the fungal serine protease proteinase K has been determined at 3.3 A resolution by single crystal X‐ray diffraction analysis. The enzyme crystallizes in the tetragonal space group P4(3)2(1)2 with cell constants a = b = 68.3 A, c = 108.5 A. The asymmetric unit consists of one monomer of 27 000 daltons mol. wt., approximately 50% higher than the so far assumed value of 18 500 daltons. The main chain fold of proteinase K shows a high degree of tertiary homology with the corresponding bacterial subtilisin BPN’. Proteinase K is the second enzyme in this family of serine proteases to be studied by X‐ray diffraction, thus confirming the existence of two unrelated families of serine proteases in pro‐and eukaryotes. |
| doi_str_mv | 10.1002/j.1460-2075.1984.tb01968.x |
| format | article |
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The enzyme crystallizes in the tetragonal space group P4(3)2(1)2 with cell constants a = b = 68.3 A, c = 108.5 A. The asymmetric unit consists of one monomer of 27 000 daltons mol. wt., approximately 50% higher than the so far assumed value of 18 500 daltons. The main chain fold of proteinase K shows a high degree of tertiary homology with the corresponding bacterial subtilisin BPN’. Proteinase K is the second enzyme in this family of serine proteases to be studied by X‐ray diffraction, thus confirming the existence of two unrelated families of serine proteases in pro‐and eukaryotes.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1984.tb01968.x</identifier><identifier>PMID: 6378621</identifier><language>eng</language><publisher>England</publisher><subject>bacteria ; Bacteria - enzymology ; crystal structure ; Endopeptidase K ; Endopeptidases - isolation & purification ; Mitosporic Fungi - enzymology ; Models, Molecular ; Protein Conformation ; serine proteinase ; Structure-Activity Relationship ; subtilisin ; Subtilisins ; Tritirachium album ; X-Ray Diffraction</subject><ispartof>The EMBO journal, 1984-06, Vol.3 (6), p.1311-1314</ispartof><rights>1984 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4248-47c38ad7866ec21f375e0d85c317e44a54e0a55df25c244b5cc6ebbc88afe8633</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC557514/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC557514/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53770,53772</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6378621$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pähler, A.</creatorcontrib><creatorcontrib>Banerjee, A.</creatorcontrib><creatorcontrib>Dattagupta, J.K.</creatorcontrib><creatorcontrib>Fujiwara, T.</creatorcontrib><creatorcontrib>Lindner, K.</creatorcontrib><creatorcontrib>Pal, G.P.</creatorcontrib><creatorcontrib>Suck, D.</creatorcontrib><creatorcontrib>Weber, G.</creatorcontrib><creatorcontrib>Saenger, W.</creatorcontrib><title>Three‐dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>The three‐dimensional structure of the fungal serine protease proteinase K has been determined at 3.3 A resolution by single crystal X‐ray diffraction analysis. The enzyme crystallizes in the tetragonal space group P4(3)2(1)2 with cell constants a = b = 68.3 A, c = 108.5 A. The asymmetric unit consists of one monomer of 27 000 daltons mol. wt., approximately 50% higher than the so far assumed value of 18 500 daltons. The main chain fold of proteinase K shows a high degree of tertiary homology with the corresponding bacterial subtilisin BPN’. Proteinase K is the second enzyme in this family of serine proteases to be studied by X‐ray diffraction, thus confirming the existence of two unrelated families of serine proteases in pro‐and eukaryotes.</description><subject>bacteria</subject><subject>Bacteria - enzymology</subject><subject>crystal structure</subject><subject>Endopeptidase K</subject><subject>Endopeptidases - isolation & purification</subject><subject>Mitosporic Fungi - enzymology</subject><subject>Models, Molecular</subject><subject>Protein Conformation</subject><subject>serine proteinase</subject><subject>Structure-Activity Relationship</subject><subject>subtilisin</subject><subject>Subtilisins</subject><subject>Tritirachium album</subject><subject>X-Ray Diffraction</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><recordid>eNqVkctu1DAUhi1E1Q6FR6gUdcEuqe9xkLooVYFeEJuythznpPUoiQfbKZ0dj8Az8iQkndGIripWxzr_Rcf6EDomuCAY05NlQbjEOcWlKEileJFqTCqpisdXaLGTXqMFppLknKjqAL2JcYkxFqok-2hfslJJShZI394HgD-_fjeuhyE6P5guiymMNo0BMt9m7TjcTbtV8AncYCJk11mABzBdzKLrXWeCS-ss-aw2NkFwc8FYJ9e56Ia3aK-dnPBuOw_R908Xt-df8ptvny_Pz25yyylXOS8tU6aZjpJgKWlZKQA3SlhGSuDcCA7YCNG0VFjKeS2slVDXVinTgpKMHaLTTe9qrHtoLAwpmE6vgutNWGtvnH6uDO5e3_kHLUQpCJ_y77f54H-MEJPuXbTQdWYAP0atCJFSyJeNhFWUqQpPxg8bow0-xgDt7hiC9YxRL_XMSs-s9IxRbzHqxyl89O93dtEtt0k_2-g_XQfr_2jWF18_Xj292V8bqLJ1</recordid><startdate>198406</startdate><enddate>198406</enddate><creator>Pähler, A.</creator><creator>Banerjee, A.</creator><creator>Dattagupta, J.K.</creator><creator>Fujiwara, T.</creator><creator>Lindner, K.</creator><creator>Pal, G.P.</creator><creator>Suck, D.</creator><creator>Weber, G.</creator><creator>Saenger, W.</creator><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>7QL</scope><scope>C1K</scope><scope>M7N</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>198406</creationdate><title>Three‐dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin</title><author>Pähler, A. ; Banerjee, A. ; Dattagupta, J.K. ; Fujiwara, T. ; Lindner, K. ; Pal, G.P. ; Suck, D. ; Weber, G. ; Saenger, W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4248-47c38ad7866ec21f375e0d85c317e44a54e0a55df25c244b5cc6ebbc88afe8633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>bacteria</topic><topic>Bacteria - enzymology</topic><topic>crystal structure</topic><topic>Endopeptidase K</topic><topic>Endopeptidases - isolation & purification</topic><topic>Mitosporic Fungi - enzymology</topic><topic>Models, Molecular</topic><topic>Protein Conformation</topic><topic>serine proteinase</topic><topic>Structure-Activity Relationship</topic><topic>subtilisin</topic><topic>Subtilisins</topic><topic>Tritirachium album</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pähler, A.</creatorcontrib><creatorcontrib>Banerjee, A.</creatorcontrib><creatorcontrib>Dattagupta, J.K.</creatorcontrib><creatorcontrib>Fujiwara, T.</creatorcontrib><creatorcontrib>Lindner, K.</creatorcontrib><creatorcontrib>Pal, G.P.</creatorcontrib><creatorcontrib>Suck, D.</creatorcontrib><creatorcontrib>Weber, G.</creatorcontrib><creatorcontrib>Saenger, W.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pähler, A.</au><au>Banerjee, A.</au><au>Dattagupta, J.K.</au><au>Fujiwara, T.</au><au>Lindner, K.</au><au>Pal, G.P.</au><au>Suck, D.</au><au>Weber, G.</au><au>Saenger, W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three‐dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1984-06</date><risdate>1984</risdate><volume>3</volume><issue>6</issue><spage>1311</spage><epage>1314</epage><pages>1311-1314</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><abstract>The three‐dimensional structure of the fungal serine protease proteinase K has been determined at 3.3 A resolution by single crystal X‐ray diffraction analysis. The enzyme crystallizes in the tetragonal space group P4(3)2(1)2 with cell constants a = b = 68.3 A, c = 108.5 A. The asymmetric unit consists of one monomer of 27 000 daltons mol. wt., approximately 50% higher than the so far assumed value of 18 500 daltons. The main chain fold of proteinase K shows a high degree of tertiary homology with the corresponding bacterial subtilisin BPN’. Proteinase K is the second enzyme in this family of serine proteases to be studied by X‐ray diffraction, thus confirming the existence of two unrelated families of serine proteases in pro‐and eukaryotes.</abstract><cop>England</cop><pmid>6378621</pmid><doi>10.1002/j.1460-2075.1984.tb01968.x</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The EMBO journal, 1984-06, Vol.3 (6), p.1311-1314 |
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| language | eng |
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| subjects | bacteria Bacteria - enzymology crystal structure Endopeptidase K Endopeptidases - isolation & purification Mitosporic Fungi - enzymology Models, Molecular Protein Conformation serine proteinase Structure-Activity Relationship subtilisin Subtilisins Tritirachium album X-Ray Diffraction |
| title | Three‐dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin |
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