Crystal Structure of Bacillus subtilis YabJ, a Purine Regulatory Protein and Member of the Highly Conserved YjgF Family
The yabJ gene in Bacillus subtillis is required for adenine-mediated repression of purine biosynthetic genes in vivo and codes for an acid-soluble, 14-kDa protein. The molecular mechanism of YabJ is unknown. YabJ is a member of a large, widely distributed family of proteins of unknown biochemical fu...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1999-11, Vol.96 (23), p.13074-13079 |
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creator | Sinha, Sangita Rappu, Pekka Lange, S. C. Mäntsälä, Pekka Zalkin, Howard Smith, Janet L. |
description | The yabJ gene in Bacillus subtillis is required for adenine-mediated repression of purine biosynthetic genes in vivo and codes for an acid-soluble, 14-kDa protein. The molecular mechanism of YabJ is unknown. YabJ is a member of a large, widely distributed family of proteins of unknown biochemical function. The 1.7- angstrom crystal structure of YabJ reveals a trimeric organization with extensive buried hydrophobic surface and an internal water-filled cavity. The most important finding in the structure is a deep, narrow cleft between subunits lined with nine side chains that are invariant among the 25 most similar homologs. This conserved site is proposed to be a binding or catalytic site for a ligand or substrate that is common to YabJ and other members of the YER057c/YjgF/UK114 family of proteins. |
doi_str_mv | 10.1073/pnas.96.23.13074 |
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This conserved site is proposed to be a binding or catalytic site for a ligand or substrate that is common to YabJ and other members of the YER057c/YjgF/UK114 family of proteins.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.96.23.13074</identifier><identifier>PMID: 10557275</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Animals ; Bacillus subtilis ; Bacillus subtilis - chemistry ; Bacillus subtilis - genetics ; Bacteria ; Bacterial Proteins - chemistry ; Biochemistry ; Biological Sciences ; Crystallography, X-Ray ; Crystals ; Humans ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Molecules ; Monomers ; Operon ; Operons ; Proteins ; Repression ; Sequence Homology, Amino Acid ; Trimers ; YabJ protein ; YjgF protein</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1999-11, Vol.96 (23), p.13074-13079</ispartof><rights>Copyright 1993-1999 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Nov 9, 1999</rights><rights>Copyright © 1999, The National Academy of Sciences 1999</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c524t-b63ec6e70f6fe29806e29d349c8f3c9767f5753abafb7cd2ea27c46274f9f3e3</citedby><cites>FETCH-LOGICAL-c524t-b63ec6e70f6fe29806e29d349c8f3c9767f5753abafb7cd2ea27c46274f9f3e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/96/23.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/49120$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/49120$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27923,27924,53790,53792,58016,58249</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10557275$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sinha, Sangita</creatorcontrib><creatorcontrib>Rappu, Pekka</creatorcontrib><creatorcontrib>Lange, S. C.</creatorcontrib><creatorcontrib>Mäntsälä, Pekka</creatorcontrib><creatorcontrib>Zalkin, Howard</creatorcontrib><creatorcontrib>Smith, Janet L.</creatorcontrib><title>Crystal Structure of Bacillus subtilis YabJ, a Purine Regulatory Protein and Member of the Highly Conserved YjgF Family</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The yabJ gene in Bacillus subtillis is required for adenine-mediated repression of purine biosynthetic genes in vivo and codes for an acid-soluble, 14-kDa protein. The molecular mechanism of YabJ is unknown. YabJ is a member of a large, widely distributed family of proteins of unknown biochemical function. The 1.7- angstrom crystal structure of YabJ reveals a trimeric organization with extensive buried hydrophobic surface and an internal water-filled cavity. The most important finding in the structure is a deep, narrow cleft between subunits lined with nine side chains that are invariant among the 25 most similar homologs. This conserved site is proposed to be a binding or catalytic site for a ligand or substrate that is common to YabJ and other members of the YER057c/YjgF/UK114 family of proteins.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bacillus subtilis</subject><subject>Bacillus subtilis - chemistry</subject><subject>Bacillus subtilis - genetics</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>Humans</subject><subject>Ligands</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Molecules</subject><subject>Monomers</subject><subject>Operon</subject><subject>Operons</subject><subject>Proteins</subject><subject>Repression</subject><subject>Sequence Homology, Amino Acid</subject><subject>Trimers</subject><subject>YabJ protein</subject><subject>YjgF protein</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFks1vEzEUxC0EoiFwRxzA4oA4kOCvtWOJC0SEgoqooJeeLK_znDhydoPtLex_z4aEquUAF_vwfjOa5zFCjymZUqL4611j81TLKeNTyokSd9CIEk0nUmhyF40IYWoyE0ycoAc5bwghupqR--iEkqpSTFUj9GOe-lxsxN9K6lzpEuDW43fWhRi7jHNXlxBDxpe2_vQKW3zepdAA_gqrLtrSph6fp7ZAaLBtlvgzbGtIe4eyBnwaVuvY43nbZEhXsMSXm9UCL-w2xP4huudtzPDoeI_RxeL9xfx0cvblw8f527OJq5gok1pycBIU8dID0zMih3PJhXYzz51WUvlKVdzW1tfKLRlYppyQTAmvPQc-Rm8Otruu3sLSQVOSjWaXwtam3rQ2mNuTJqzNqr0yjGvCBvmLozy13zvIxWxDdhCjbaDtspGaKSn5_0GqBFF0SDpGz_8CN22XmuEJDCOUV1qLvRs5QC61OSfw14EpMfvizb54o-UQ0_wufpA8vbnoDcGh6QF4dgT20j_j2xYv_00Y38VY4GcZ0CcHdJOHP3DNCk0Z4b8Af0DM0w</recordid><startdate>19991109</startdate><enddate>19991109</enddate><creator>Sinha, Sangita</creator><creator>Rappu, Pekka</creator><creator>Lange, S. 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C. ; Mäntsälä, Pekka ; Zalkin, Howard ; Smith, Janet L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c524t-b63ec6e70f6fe29806e29d349c8f3c9767f5753abafb7cd2ea27c46274f9f3e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bacillus subtilis</topic><topic>Bacillus subtilis - chemistry</topic><topic>Bacillus subtilis - genetics</topic><topic>Bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Biochemistry</topic><topic>Biological Sciences</topic><topic>Crystallography, X-Ray</topic><topic>Crystals</topic><topic>Humans</topic><topic>Ligands</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Molecules</topic><topic>Monomers</topic><topic>Operon</topic><topic>Operons</topic><topic>Proteins</topic><topic>Repression</topic><topic>Sequence Homology, Amino Acid</topic><topic>Trimers</topic><topic>YabJ protein</topic><topic>YjgF protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sinha, Sangita</creatorcontrib><creatorcontrib>Rappu, Pekka</creatorcontrib><creatorcontrib>Lange, S. 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The 1.7- angstrom crystal structure of YabJ reveals a trimeric organization with extensive buried hydrophobic surface and an internal water-filled cavity. The most important finding in the structure is a deep, narrow cleft between subunits lined with nine side chains that are invariant among the 25 most similar homologs. This conserved site is proposed to be a binding or catalytic site for a ligand or substrate that is common to YabJ and other members of the YER057c/YjgF/UK114 family of proteins.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>10557275</pmid><doi>10.1073/pnas.96.23.13074</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Bacillus subtilis Bacillus subtilis - chemistry Bacillus subtilis - genetics Bacteria Bacterial Proteins - chemistry Biochemistry Biological Sciences Crystallography, X-Ray Crystals Humans Ligands Models, Molecular Molecular Sequence Data Molecules Monomers Operon Operons Proteins Repression Sequence Homology, Amino Acid Trimers YabJ protein YjgF protein |
title | Crystal Structure of Bacillus subtilis YabJ, a Purine Regulatory Protein and Member of the Highly Conserved YjgF Family |
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