4RR5

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

Summary for 4RR5

• Entry DOI: 10.2210/pdb4rr5/pdb
• Descriptor: Malonyl CoA-acyl carrier protein transacylase, ACETATE ION (3 entities in total)
• Functional Keywords: hydrolase, transferase
• Biological source: Synechocystis sp. PCC 6803 substr. Kazusa
• Total number of polymer chains: 1
• Total formula weight: 31574.74

Authors

Liu, Y. (deposition date: 2014-11-06, release date: 2015-07-01, Last modification date: 2023-11-08)

Primary citation

Liu, Y.,Feng, Y.,Wang, Y.,Li, X.,Cao, X.,Xue, S.
Structural and biochemical characterization of MCAT from photosynthetic microorganism Synechocystis sp. PCC 6803 reveal its stepwise catalytic mechanism
Biochem.Biophys.Res.Commun., 457:398-403, 2015

PubMed Abstract: 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 Å 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.

PubMed: 25582772
DOI: 10.1016/j.bbrc.2015.01.003

Experimental method

X-RAY DIFFRACTION (2.427 Å)