3HYK

2.31 Angstrom resolution crystal structure of a holo-(acyl-carrier-protein) synthase from Bacillus anthracis str. Ames in complex with CoA (3',5'-ADP)

3HYK の概要

• エントリーDOI: 10.2210/pdb3hyk/pdb
• 関連するPDBエントリー: 1F7L 3F09
• 分子名称: Holo-[acyl-carrier-protein] synthase, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: holo-(acyl-carrier-protein) synthase, structural genomics, infectious diseases, center for structural genomics of infectious diseases, fatty acid biosynthesis, lipid synthesis, magnesium, metal-binding, transferase, csgid
• 由来する生物種: Bacillus anthracis (anthrax,anthrax bacterium)
• 細胞内の位置: Cytoplasm : Q81JG3
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 43593.95

構造登録者

Halavaty, A.S.,Minasov, G.,Skarina, T.,Onopriyenko, O.,Papazisi, L.,Savchenko, A.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2009-06-22, 公開日: 2009-06-30, 最終更新日: 2024-10-16)

主引用文献

Halavaty, A.S.,Kim, Y.,Minasov, G.,Shuvalova, L.,Dubrovska, I.,Winsor, J.,Zhou, M.,Onopriyenko, O.,Skarina, T.,Papazisi, L.,Kwon, K.,Peterson, S.N.,Joachimiak, A.,Savchenko, A.,Anderson, W.F.
Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria.
Acta Crystallogr.,Sect.D, 68:1359-1370, 2012

PubMed Abstract: Some bacterial type II fatty-acid synthesis (FAS II) enzymes have been shown to be important candidates for drug discovery. The scientific and medical quest for new FAS II protein targets continues to stimulate research in this field. One of the possible additional candidates is the acyl-carrier-protein synthase (AcpS) enzyme. Its holo form post-translationally modifies the apo form of an acyl carrier protein (ACP), which assures the constant delivery of thioester intermediates to the discrete enzymes of FAS II. At the Center for Structural Genomics of Infectious Diseases (CSGID), AcpSs from Staphylococcus aureus (AcpS(SA)), Vibrio cholerae (AcpS(VC)) and Bacillus anthracis (AcpS(BA)) have been structurally characterized in their apo, holo and product-bound forms, respectively. The structure of AcpS(BA) is emphasized because of the two 3',5'-adenosine diphosphate (3',5'-ADP) product molecules that are found in each of the three coenzyme A (CoA) binding sites of the trimeric protein. One 3',5'-ADP is bound as the 3',5'-ADP part of CoA in the known structures of the CoA-AcpS and 3',5'-ADP-AcpS binary complexes. The position of the second 3',5'-ADP has never been described before. It is in close proximity to the first 3',5'-ADP and the ACP-binding site. The coordination of two ADPs in AcpS(BA) may possibly be exploited for the design of AcpS inhibitors that can block binding of both CoA and ACP.

PubMed: 22993090
DOI: 10.1107/S0907444912029101

実験手法

X-RAY DIFFRACTION (2.31 Å)