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[[Image:3asb.jpg|left|200px]]
==Crystal structure of PLP-bound LL-diaminopimelate aminotransferase from Chlamydia trachomatis==
<StructureSection load='3asb' size='340' side='right' caption='[[3asb]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== 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>
</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><br>
<tr><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><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>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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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===Crystal structure of PLP-bound LL-diaminopimelate aminotransferase from Chlamydia trachomatis===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
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== References ==
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==About this Structure==
[[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].
 
==Reference==
<ref group="xtra">PMID:021722650</ref><references group="xtra"/>
[[Category: Chlamydia trachomatis]]
[[Category: Chlamydia trachomatis]]
[[Category: LL-diaminopimelate aminotransferase]]
[[Category: LL-diaminopimelate aminotransferase]]