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| ==Carbapenam Synthetase== | | ==Carbapenam Synthetase== |
| <StructureSection load='1q15' size='340' side='right' caption='[[1q15]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1q15' size='340' side='right'caption='[[1q15]], [[Resolution|resolution]] 2.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1q15]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_carotovorus"_jones_1901 "bacillus carotovorus" jones 1901]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q15 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q15 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1q15]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q15 FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q19|1q19]]</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]] 2.3Å</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=1q15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q15 OCA], [http://pdbe.org/1q15 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q15 RCSB], [http://www.ebi.ac.uk/pdbsum/1q15 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q15 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=1q15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q15 OCA], [https://pdbe.org/1q15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q15 RCSB], [https://www.ebi.ac.uk/pdbsum/1q15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q15 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/CARA_PECCA CARA_PECCA]] Involved in the biosynthesis of carbapenam-3-carboxylate, a beta-lactam antibiotic of the carbapenem class. Catalyzes the ATP-dependent formation of (3S,5S)-carbapenam-3-carboxylate from (2S,5S)-5-carboxymethylproline.<ref>PMID:12820893</ref> <ref>PMID:17658887</ref> <ref>PMID:19371088</ref> | | [https://www.uniprot.org/uniprot/CARA_PECCC CARA_PECCC] Involved in the biosynthesis of carbapenam-3-carboxylate, a beta-lactam antibiotic of the carbapenem class. Catalyzes the ATP-dependent formation of (3S,5S)-carbapenam-3-carboxylate from (2S,5S)-5-carboxymethylproline.<ref>PMID:12820893</ref> <ref>PMID:17658887</ref> <ref>PMID:19371088</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1q15 ConSurf]. | | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1q15 ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Carbapenam synthetase (CarA) is an ATP/Mg2+-dependent enzyme that catalyzes formation of the beta-lactam ring in (5R)-carbapenem-3-carboxylic acid biosynthesis. CarA is homologous to beta-lactam synthetase (beta-LS), which is involved in clavulanic acid biosynthesis. The catalytic cycles of CarA and beta-LS mediate substrate adenylation followed by beta-lactamization via a tetrahedral intermediate or transition state. Another member of this family of ATP/Mg2+-dependent enzymes, asparagine synthetase (AS-B), catalyzes intermolecular, rather than intramolecular, amide bond formation in asparagine biosynthesis. The crystal structures of apo-CarA and CarA complexed with the substrate (2S,5S)-5-carboxymethylproline (CMPr), ATP analog alpha,beta-methyleneadenosine 5'-triphosphate (AMP-CPP), and a single Mg2+ ion have been determined. CarA forms a tetramer. Each monomer resembles beta-LS and AS-B in overall fold, but key differences are observed. The N-terminal domain lacks the glutaminase active site found in AS-B, and an extended loop region not observed in beta-LS or AS-B is present. Comparison of the C-terminal synthetase active site to that in beta-LS reveals that the ATP binding site is highly conserved. By contrast, variations in the substrate binding pocket reflect the different substrates of the two enzymes. The Mg2+ coordination is also different. Several key residues in the active site are conserved between CarA and beta-LS, supporting proposed roles in beta-lactam formation. These data provide further insight into the structures of this class of enzymes and suggest that CarA might be a versatile target for protein engineering experiments aimed at developing improved production methods and new carbapenem antibiotics.
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| Crystal structure of carbapenam synthetase (CarA).,Miller MT, Gerratana B, Stapon A, Townsend CA, Rosenzweig AC J Biol Chem. 2003 Oct 17;278(42):40996-1002. Epub 2003 Jul 30. PMID:12890666<ref>PMID:12890666</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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| <div class="pdbe-citations 1q15" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus carotovorus jones 1901]] | | [[Category: Large Structures]] |
| [[Category: Gerratana, B]] | | [[Category: Pectobacterium carotovorum]] |
| [[Category: Miller, M T]] | | [[Category: Gerratana B]] |
| [[Category: Rosenzweig, A C]] | | [[Category: Miller MT]] |
| [[Category: Stapon, A]] | | [[Category: Rosenzweig AC]] |
| [[Category: Townsend, C A]] | | [[Category: Stapon A]] |
| [[Category: Amp-cpp]] | | [[Category: Townsend CA]] |
| [[Category: As-b]]
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| [[Category: B-l]]
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| [[Category: B-lactam synthetase]]
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| [[Category: B-methyleneadenosine 5-triphosphate]]
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| [[Category: Biosynthetic protein]]
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| [[Category: Cea]]
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| [[Category: Class b asparagine synthetase]]
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| [[Category: Cma]]
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| [[Category: Cmpr]]
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| [[Category: Some]]
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