4rr5
From Proteopedia
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| - | ''' | + | ==The crystal structure of Synechocystis sp. PCC 6803 Malonyl-CoA: ACP Transacylase== |
| + | <StructureSection load='4rr5' size='340' side='right' caption='[[4rr5]], [[Resolution|resolution]] 2.43Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4rr5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RR5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RR5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] </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=4rr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rr5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rr5 RCSB], [http://www.ebi.ac.uk/pdbsum/4rr5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Malonyl-coenzyme A: acyl-carrier protein transacylase (MCAT) catalyzes the transfer of malonyl group from malonyl-CoA to the holo-acyl carrier protein (Holo-ACP), yielding malonyl-ACP. The overall reaction has been extensively studied in heterotrophic microorganisms, while its mechanism in photosynthetic autotrophs as well as the stepwise reaction information remains unclear. Here the 2.42 A crystal structure of MCAT from photosynthetic microorganism Synechocystis sp. PCC 6803 is presented. It demonstrates that Arg113, Ser88 and His188 constitute catalytic triad. The second step involved ACP-MCAT-malonyl intermediate is speed-limited instead of the malonyl-CoA-MCAT intermediate in the first step. Therefore His87, Arg113 and Ser88 render different contributions for the two intermediates. Additionally, S88T mutant initializes the reaction by H87 deprotonating S88T which is different from the wild type. | ||
| - | + | Structural and biochemical characterization of MCAT from photosynthetic microorganism Synechocystis sp. PCC 6803 reveal its stepwise catalytic mechanism.,Liu Y, Feng Y, Wang Y, Li X, Cao X, Xue S Biochem Biophys Res Commun. 2015 Feb 13;457(3):398-403. doi:, 10.1016/j.bbrc.2015.01.003. Epub 2015 Jan 9. PMID:25582772<ref>PMID:25582772</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Liu, Y]] | [[Category: Liu, Y]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 12:14, 1 July 2015
The crystal structure of Synechocystis sp. PCC 6803 Malonyl-CoA: ACP Transacylase
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