2a81

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[[Image:2a81.png|left|200px]]
 
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{{STRUCTURE_2a81| PDB=2a81 | SCENE= }}
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==carboxymethylproline synthase (CarB) from pectobacterium carotovora, complexed with acetyl CoA and bicine==
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<StructureSection load='2a81' size='340' side='right'caption='[[2a81]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2a81]] is a 3 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=2A81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A81 FirstGlance]. <br>
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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]] 3.15&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=BCN:BICINE'>BCN</scene></td></tr>
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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=2a81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a81 OCA], [https://pdbe.org/2a81 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a81 RCSB], [https://www.ebi.ac.uk/pdbsum/2a81 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a81 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CARB_PECCC CARB_PECCC] Catalyzes the formation of (2S,5S)-carboxymethylproline (t-CMP) from malonyl-CoA and (S)-1-pyrroline-5-carboxylate, the first step in the biosynthesis of (5R)-carbapen-2-em-3-carboxylate, a beta-lactam antibiotic of the carbapenem class (PubMed:15595850, PubMed:14625287). Also catalyzes the independent decarboxylation of malonyl-CoA and methylmalonyl-CoA and the hydrolysis of CoA esters such as acetyl-CoA and propionyl-CoA (PubMed:15595850). Catalyzes the reaction with a C2 epimeric mixture of methylmalonyl-CoA to give a 55:45 mixture of (6R)- and (6S)-epimers of 6-methyl-t-CMP, under standard incubation conditions (PubMed:21505494).<ref>PMID:14625287</ref> <ref>PMID:15595850</ref> <ref>PMID:15726176</ref> <ref>PMID:18972478</ref> <ref>PMID:21505494</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/2a81_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2a81 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The first step in the biosynthesis of the medicinally important carbapenem family of beta-lactam antibiotics is catalyzed by carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily. CarB catalyzes formation of (2S,5S)-carboxymethylproline [(2S,5S)-t-CMP] from malonyl-CoA and l-glutamate semialdehyde. In addition to using a cosubstrate, CarB catalyzes C-C and C-N bond formation processes as well as an acyl-coenzyme A hydrolysis reaction. We describe the crystal structure of CarB in the presence and absence of acetyl-CoA at 2.24 A and 3.15 A resolution, respectively. The structures reveal that CarB contains a conserved oxy-anion hole probably required for decarboxylation of malonyl-CoA and stabilization of the resultant enolate. Comparison of the structures reveals that conformational changes (involving His(229)) in the cavity predicted to bind l-glutamate semialdehyde occur on (co)substrate binding. Mechanisms for the formation of the carboxymethylproline ring are discussed in the light of the structures and the accompanying studies using isotopically labeled substrates; cyclization via 1,4-addition is consistent with the observed labeling results (providing that hydrogen exchange at the C-6 position of carboxymethylproline does not occur). The side chain of Glu(131) appears to be positioned to be involved in hydrolysis of the carboxymethylproline-CoA ester intermediate. Labeling experiments ruled out the possibility that hydrolysis proceeds via an anhydride in which water attacks a carbonyl derived from Glu(131), as proposed for 3-hydroxyisobutyryl-CoA hydrolase. The structural work will aid in mutagenesis studies directed at altering the selectivity of CarB to provide intermediates for the production of clinically useful carbapenems.
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===carboxymethylproline synthase (CarB) from pectobacterium carotovora, complexed with acetyl CoA and bicine===
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Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis.,Sleeman MC, Sorensen JL, Batchelar ET, McDonough MA, Schofield CJ J Biol Chem. 2005 Oct 14;280(41):34956-65. Epub 2005 Aug 11. PMID:16096274<ref>PMID:16096274</ref>
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{{ABSTRACT_PUBMED_16096274}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2a81" style="background-color:#fffaf0;"></div>
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[[2a81]] is a 3 chain structure with 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=2A81 OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:016096274</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pectobacterium carotovorum]]
[[Category: Pectobacterium carotovorum]]
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[[Category: Batchelar, E T.]]
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[[Category: Batchelar ET]]
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[[Category: McDonough, M A.]]
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[[Category: McDonough MA]]
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[[Category: Schofield, C J.]]
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[[Category: Schofield CJ]]
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[[Category: Sleeman, M C.]]
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[[Category: Sleeman MC]]
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[[Category: Sorensen, J L.]]
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[[Category: Sorensen JL]]
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[[Category: Acetyl coenzyme some]]
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[[Category: Antibiotic]]
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[[Category: Beta-lactam]]
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[[Category: Bicine]]
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[[Category: Biosynthetic protein]]
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[[Category: Carbapenam]]
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[[Category: Carbapenem]]
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[[Category: Crotonase]]
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Current revision

carboxymethylproline synthase (CarB) from pectobacterium carotovora, complexed with acetyl CoA and bicine

PDB ID 2a81

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