4rr5 | pdb_00004rr5

The crystal structure of Synechocystis sp. PCC 6803 Malonyl-CoA: ACP Transacylase

spinqualitylabelsall models 4rr5, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rr5 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT Activity: [Acyl-carrier-protein_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number 2.3.1.39 Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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