3ftt

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Crystal Structure of the galactoside O-acetyltransferase from Staphylococcus aureusCrystal Structure of the galactoside O-acetyltransferase from Staphylococcus aureus

Structural highlights

3ftt is a 1 chain structure with sequence from Staphylococcus aureus subsp. aureus COL. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

ATRF2_STAAC

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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 LbetaH domain. CoA binds in the active site formed by the residues from adjacent LbetaH 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.

Biophysical analysis of the putative acetyltransferase SACOL2570 from methicillin-resistant Staphylococcus aureus.,Luo HB, Knapik AA, Petkowski JJ, Demas M, Shumilin IA, Zheng H, Chruszcz M, Minor W J Struct Funct Genomics. 2013 Sep;14(3):97-108. doi: 10.1007/s10969-013-9158-6., Epub 2013 Aug 21. PMID:23963951[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Luo HB, Knapik AA, Petkowski JJ, Demas M, Shumilin IA, Zheng H, Chruszcz M, Minor W. Biophysical analysis of the putative acetyltransferase SACOL2570 from methicillin-resistant Staphylococcus aureus. J Struct Funct Genomics. 2013 Sep;14(3):97-108. doi: 10.1007/s10969-013-9158-6., Epub 2013 Aug 21. PMID:23963951 doi:http://dx.doi.org/10.1007/s10969-013-9158-6

3ftt, resolution 1.60Å

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OCA