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1q15

From Proteopedia

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[[Image:1q15.gif|left|200px]]
 
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{{Structure
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==Carbapenam Synthetase==
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|PDB= 1q15 |SIZE=350|CAPTION= <scene name='initialview01'>1q15</scene>, resolution 2.30&Aring;
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<StructureSection load='1q15' size='340' side='right'caption='[[1q15]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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|GENE=
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<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>
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}}
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</table>
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== Function ==
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'''Carbapenam Synthetase'''
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q1/1q15_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1Q15 is a [[Single protein]] structure of sequence from [http://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].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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].
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12890666 12890666]
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pectobacterium carotovorum]]
[[Category: Pectobacterium carotovorum]]
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[[Category: Single protein]]
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[[Category: Gerratana B]]
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[[Category: Gerratana, B.]]
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[[Category: Miller MT]]
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[[Category: Miller, M T.]]
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[[Category: Rosenzweig AC]]
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[[Category: Rosenzweig, A C.]]
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[[Category: Stapon A]]
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[[Category: Stapon, A.]]
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[[Category: Townsend CA]]
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[[Category: Townsend, C A.]]
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[[Category: (2]]
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[[Category: 5s)-5-carboxymethylproline; b-l]]
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[[Category: some]]
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[[Category: b-lactam synthetase; as-b]]
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[[Category: b-methyleneadenosine 5-triphosphate; cea]]
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[[Category: class b asparagine synthetase; amp-cpp]]
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[[Category: cmpr]]
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[[Category: n2-(carboxyethyl)-l-arginine; cma]]
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[[Category: n2-(carboxylmethyl)-l-arginine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:31:38 2008''
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Current revision

Carbapenam Synthetase

PDB ID 1q15

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