4JM7

1.82 Angstrom resolution crystal structure of holo-(acyl-carrier-protein) synthase (acpS) from Staphylococcus aureus

Replaces:  3F09

Summary for 4JM7

• Entry DOI: 10.2210/pdb4jm7/pdb
• Related: 3F09
• Descriptor: Holo-[acyl-carrier-protein] synthase (2 entities in total)
• Functional Keywords: holo-(acyl-carrier-protein) synthase, structural genomics, infectious deseases, fatty acid biosynthesis, lipid synthesis, magnesium, metal-binding, transferase, center for structural genomics of infectious diseases, csgid, niaid, national institute of allergy and infectious diseases
• Biological source: Staphylococcus aureus
• Cellular location: Cytoplasm : Q5HED0
• Total number of polymer chains: 3
• Total formula weight: 49114.50

Authors

Halavaty, A.S.,Minasov, G.,Shuvalova, L.,Dubrovska, I.,Papazisi, L.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2013-03-13, release date: 2013-03-27, Last modification date: 2023-09-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.824 Å)