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3asb

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Revision as of 07:07, 15 April 2020

Crystal structure of PLP-bound LL-diaminopimelate aminotransferase from Chlamydia trachomatis

Structural highlights

3asb is a 1 chain structure with sequence from "chlamydozoon_trachomatis"_(busacca_1935)_moshkovski_1945 "chlamydozoon trachomatis" (busacca 1935) moshkovski 1945. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	3asa
Gene:	dapL, aspC, CT_390 ("Chlamydozoon trachomatis" (Busacca 1935) Moshkovski 1945)
Activity:	LL-diaminopimelate aminotransferase, with EC number 2.6.1.83
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3asb"

@@ Line 1: / Line 1: @@
 ==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=''>
+<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/"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=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/"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=3ASB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3ASB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
+</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3asa|3asa]]</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 "Chlamydozoon trachomatis" (Busacca 1935) Moshkovski 1945])</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 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://pdbe.org/3asb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3asb RCSB], [http://www.ebi.ac.uk/pdbsum/3asb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3asb ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3asb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asb OCA], [http://pdbe.org/3asb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3asb RCSB], [http://www.ebi.ac.uk/pdbsum/3asb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3asb ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 </StructureSection>
 [[Category: LL-diaminopimelate aminotransferase]]
+[[Category: Large Structures]]
 [[Category: James, M N]]
 [[Category: Watanabe, N]]
 [[Category: Plp dependent aminotransferase]]
 [[Category: Transferase]]

3asb

From Proteopedia

Revision as of 07:07, 15 April 2020

Crystal structure of PLP-bound LL-diaminopimelate aminotransferase from Chlamydia trachomatis

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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