3V4E

Crystal Structure of the galactoside O-acetyltransferase in complex with CoA

Summary for 3V4E

• Entry DOI: 10.2210/pdb3v4e/pdb
• Related: 3FTT
• Descriptor: Galactoside O-acetyltransferase, DI(HYDROXYETHYL)ETHER, TRIETHYLENE GLYCOL, ... (6 entities in total)
• Functional Keywords: structural genomics, center for structural genomics of infectious diseases, csgid, galactoside o-acetyltransferase, coa, transferase
• Biological source: Staphylococcus aureus subsp. aureus
• Total number of polymer chains: 3
• Total formula weight: 69906.34

Authors

Knapik, A.A.,Shumilin, I.A.,Luo, H.-B.,Chruszcz, M.,Zimmerman, M.D.,Cymborowski, M.,Anderson, W.F.,Minor, W.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2011-12-14, release date: 2012-01-11, Last modification date: 2023-09-13)

Primary citation

Luo, H.B.,Knapik, A.A.,Petkowski, J.J.,Demas, M.,Shumilin, I.A.,Zheng, H.,Chruszcz, M.,Minor, W.
Biophysical analysis of the putative acetyltransferase SACOL2570 from methicillin-resistant Staphylococcus aureus.
J.Struct.Funct.Genom., 14:97-108, 2013

PubMed Abstract: Methicillin-resistant Staphylococcus aureus (MRSA) is a major cause of a myriad of insidious and intractable infections in humans, especially in patients with compromised immune systems and children. Here, we report the apo- and CoA-bound crystal structures of a member of the galactoside acetyltransferase superfamily from methicillin-resistant S. aureus SACOL2570 which was recently shown to be down regulated in S. aureus grown in the presence of fusidic acid, an antibiotic used to treat MRSA infections. SACOL2570 forms a homotrimer in solution, as confirmed by small-angle X-ray scattering and dynamic light scattering. The protein subunit consists of an N-terminal alpha-helical domain connected to a C-terminal LβH domain. CoA binds in the active site formed by the residues from adjacent LβH domains. After determination of CoA-bound structure, molecular dynamics simulations were performed to model the binding of AcCoA. Binding of both AcCoA and CoA to SACOL2570 was verified by isothermal titration calorimetry. SACOL2570 most likely acts as an acetyltransferase, using AcCoA as an acetyl group donor and an as-yet-undetermined chemical moiety as an acceptor. SACOL2570 was recently used as a scaffold for mutations that lead the generation of cage-like assemblies, and has the potential to be used for the generation of more complex nanostructures.

PubMed: 23963951
DOI: 10.1007/s10969-013-9158-6

Experimental method

X-RAY DIFFRACTION (1.95 Å)