3asa

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==Crystal structure of apo-LL-diaminopimelate aminotransferase from Chlamydia trachomatis==
==Crystal structure of apo-LL-diaminopimelate aminotransferase from Chlamydia trachomatis==
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<StructureSection load='3asa' size='340' side='right' caption='[[3asa]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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<StructureSection load='3asa' size='340' side='right'caption='[[3asa]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3asa]] 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=3ASA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ASA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3asa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ASA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ASA FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3asb|3asb]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3asa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asa OCA], [https://pdbe.org/3asa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3asa RCSB], [https://www.ebi.ac.uk/pdbsum/3asa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3asa ProSAT]</span></td></tr>
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<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>
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</table>
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<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=3asa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3asa RCSB], [http://www.ebi.ac.uk/pdbsum/3asa PDBsum]</span></td></tr>
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== Function ==
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<table>
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[https://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We have previously reported the structures of the native holo and substrate-bound forms of ll-diaminopimelate aminotransferase from Arabidopsis thaliana (AtDAP-AT). Here, we report the crystal and molecular structures of the ll-diaminopimelate aminotransferase from Chlamydia trachomatis (CtDAP-AT) in the apo-form and the pyridoxal-5'-phosphate-bound form. The molecular structure of CtDAP-AT shows that its overall fold is essentially identical with that of AtDAP-AT except that CtDAP-AT adopts an "open" conformation as opposed to the "closed" conformation of AtDAP-AT. Although AtDAP-AT and CtDAP-AT are approximately 40% identical in their primary sequence, they have major differences in their substrate specificities; AtDAP-AT is highly specific for LL-DAP, whereas CtDAP-AT accepts a wider range of substrates. Since all of the residues involved in substrate recognition are highly conserved between AtDAP-AT and CtDAP-AT, we propose that differences in flexibility of the loops lining the active-site region between the two enzymes likely account for the differences in substrate specificity.
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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>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Chlamydia trachomatis]]
[[Category: Chlamydia trachomatis]]
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[[Category: LL-diaminopimelate aminotransferase]]
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[[Category: Large Structures]]
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[[Category: James, M N.]]
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[[Category: James MN]]
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[[Category: Watanabe, N.]]
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[[Category: Watanabe N]]
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[[Category: Plp dependent aminotransferase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of apo-LL-diaminopimelate aminotransferase from Chlamydia trachomatis

PDB ID 3asa

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