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| | <StructureSection load='3asa' size='340' side='right'caption='[[3asa]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='3asa' size='340' side='right'caption='[[3asa]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3asa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"chlamydozoon_trachomatis"_(busacca_1935)_moshkovski_1945 "chlamydozoon trachomatis" (busacca 1935) moshkovski 1945]. 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> | + | <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> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3asb|3asb]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapL, aspC, CT_390 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=813 "Chlamydozoon trachomatis" (Busacca 1935) Moshkovski 1945])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/LL-diaminopimelate_aminotransferase LL-diaminopimelate aminotransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.83 2.6.1.83] </span></td></tr>
| + | |
| | <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> | | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: LL-diaminopimelate aminotransferase]] | + | [[Category: Chlamydia trachomatis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: James, M N]] | + | [[Category: James MN]] |
| - | [[Category: Watanabe, N]] | + | [[Category: Watanabe N]] |
| - | [[Category: Plp dependent aminotransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
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.[1]
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McCoy AJ, Adams NE, Hudson AO, Gilvarg C, Leustek T, Maurelli AT. L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate/lysine. Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17909-14. Epub 2006 Nov 8. PMID:17093042 doi:http://dx.doi.org/10.1073/pnas.0608643103
- ↑ Watanabe N, Clay MD, van Belkum MJ, Fan C, Vederas JC, James MN. The Structure of ll-Diaminopimelate Aminotransferase from Chlamydia trachomatis: Implications for Its Broad Substrate Specificity. J Mol Biol. 2011 Aug 19;411(3):649-60. Epub 2011 Jun 21. PMID:21722650 doi:10.1016/j.jmb.2011.06.023
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