PDBsum entry 3ftt

Transferase

PDB id: 3ftt

Contents

Protein chain

188 a.a. *

Waters ×218

* Residue conservation analysis

PDB id:

3ftt

Name:

Transferase

Title:

Crystal structure of the galactoside o-acetyltransferase from staphylococcus aureus

Structure:

Putative acetyltransferase sacol2570. Chain: a. Engineered: yes

Source:

Staphylococcus aureus subsp. Aureus col. Organism_taxid: 93062. Gene: sacol2570. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.60Å R-factor: 0.160 R-free: 0.187

Authors:

A.A.Knapik,I.A.Shumilin,H.Cui,X.Xu,M.Chruszcz,M.D.Zimmerman, M.Cymborowski,W.F.Anderson,A.Savchenko,W.Minor,Center For Structural Genomics Of Infectious Diseases (Csgid)

Key ref:

H.B.Luo et al. (2013). Biophysical analysis of the putative acetyltransferase SACOL2570 from methicillin-resistant Staphylococcus aureus. J Struct Funct Genomics, 14, 97. PubMed id: 23963951

Date:

13-Jan-09 Release date: 03-Mar-09

Protein chain

Q5HCZ5  (ATRF2_STAAC) -  Putative acetyltransferase SACOL2570 from Staphylococcus aureus (strain COL)

Seq: 199 a.a.

Struc: 188 a.a.

Enzyme reactions

• Enzyme class: E.C.2.3.1.- - ?????

J Struct Funct Genomics 14:97 (2013)

PubMed id: 23963951

Biophysical analysis of the putative acetyltransferase SACOL2570 from methicillin-resistant Staphylococcus aureus.

H.B.Luo, A.A.Knapik, J.J.Petkowski, M.Demas, I.A.Shumilin, H.Zheng, M.Chruszcz, W.Minor.

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.