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3asb
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3asb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ASB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ASB FirstGlance]. <br> | <table><tr><td colspan='2'>[[3asb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ASB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ASB FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3asa|3asa]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3asa|3asa]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapL, aspC, CT_390 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=813 Chlamydia trachomatis])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapL, aspC, CT_390 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=813 Chlamydia trachomatis])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/LL-diaminopimelate_aminotransferase LL-diaminopimelate aminotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.83 2.6.1.83] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/LL-diaminopimelate_aminotransferase LL-diaminopimelate aminotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.83 2.6.1.83] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3asb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3asb RCSB], [http://www.ebi.ac.uk/pdbsum/3asb PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3asb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3asb RCSB], [http://www.ebi.ac.uk/pdbsum/3asb PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DAPAT_CHLTR DAPAT_CHLTR]] Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate, a reaction that requires three enzymes in E.coli. Is also able to use meso-diaminopimelate, cystathionine, lysine or ornithine as substrates.<ref>PMID:17093042</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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The Structure of ll-Diaminopimelate Aminotransferase from Chlamydia trachomatis: Implications for Its Broad Substrate Specificity.,Watanabe N, Clay MD, van Belkum MJ, Fan C, Vederas JC, James MN J Mol Biol. 2011 Aug 19;411(3):649-60. Epub 2011 Jun 21. PMID:21722650<ref>PMID:21722650</ref> | The Structure of ll-Diaminopimelate Aminotransferase from Chlamydia trachomatis: Implications for Its Broad Substrate Specificity.,Watanabe N, Clay MD, van Belkum MJ, Fan C, Vederas JC, James MN J Mol Biol. 2011 Aug 19;411(3):649-60. Epub 2011 Jun 21. PMID:21722650<ref>PMID:21722650</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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[[Category: Chlamydia trachomatis]] | [[Category: Chlamydia trachomatis]] | ||
[[Category: LL-diaminopimelate aminotransferase]] | [[Category: LL-diaminopimelate aminotransferase]] | ||
| - | [[Category: James, M N | + | [[Category: James, M N]] |
| - | [[Category: Watanabe, N | + | [[Category: Watanabe, N]] |
[[Category: Plp dependent aminotransferase]] | [[Category: Plp dependent aminotransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 22:24, 24 December 2014
Crystal structure of PLP-bound LL-diaminopimelate aminotransferase from Chlamydia trachomatis
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