1twi: Difference between revisions
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<StructureSection load='1twi' size='340' side='right'caption='[[1twi]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1twi' size='340' side='right'caption='[[1twi]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1twi]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1twi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TWI FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=1twi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1twi OCA], [https://pdbe.org/1twi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1twi RCSB], [https://www.ebi.ac.uk/pdbsum/1twi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1twi ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1twi TOPSAN]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/DCDA_METJA DCDA_METJA] Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.<ref>PMID:12429091</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: | [[Category: Bonanno JB]] | ||
[[Category: | [[Category: Burley SK]] | ||
[[Category: Lencastre | [[Category: De Lencastre H]] | ||
[[Category: | [[Category: He G]] | ||
[[Category: Pinho | [[Category: Pinho MG]] | ||
[[Category: Rajashankar | [[Category: Rajashankar KR]] | ||
[[Category: Ray | [[Category: Ray SS]] | ||
[[Category: Tomasz | [[Category: Tomasz A]] | ||
Latest revision as of 09:34, 23 August 2023
Crystal structure of Diaminopimelate Decarboxylase from m. jannaschii in co-complex with L-lysineCrystal structure of Diaminopimelate Decarboxylase from m. jannaschii in co-complex with L-lysine
Structural highlights
FunctionDCDA_METJA Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCocrystal structures of Methanococcus jannaschii diaminopimelate decarboxylase (DAPDC) bound to a substrate analog, azelaic acid, and its L-lysine product have been determined at 2.6 A and 2.0 A, respectively. This PLP-dependent enzyme is responsible for the final step of L-lysine biosynthesis in bacteria and plays a role in beta-lactam antibiotic resistance in Staphylococcus aureus. Substrate specificity derives from recognition of the L-chiral center of diaminopimelate and a system of ionic "molecular rulers" that dictate substrate length. A coupled-enzyme assay system permitted measurement of kinetic parameters for recombinant DAPDCs and inhibition constants (K(i)) for azelaic acid (89 microM) and other substrate analogs. Implications for rational design of broad-spectrum antimicrobial agents targeted against DAPDCs of drug-resistant strains of bacterial pathogens, such as Staphylococcus aureus, are discussed. Cocrystal structures of diaminopimelate decarboxylase: mechanism, evolution, and inhibition of an antibiotic resistance accessory factor.,Ray SS, Bonanno JB, Rajashankar KR, Pinho MG, He G, De Lencastre H, Tomasz A, Burley SK Structure. 2002 Nov;10(11):1499-508. PMID:12429091[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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