PDBsum entry 4lua

Transferase

PDB id: 4lua

Contents

Protein chain

156 a.a.

Ligands

GOL

Waters ×154

PDB id:

4lua

Name:

Transferase

Title:

Crystal structure of n-acetyltransferase from staphylococcus aureus mu50

Structure:

N-acetyltransferase. Chain: a. Engineered: yes

Source:

Staphylococcus aureus subsp. Aureus. Organism_taxid: 158878. Strain: mu50. Gene: sav0826. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.60Å R-factor: 0.180 R-free: 0.208

Authors:

P.Srivastava,J.K.Forwood

Key ref:

P.Srivastava et al. (2014). Purification, crystallization and preliminary X-ray diffraction analysis of the N-acetyltransferase SAV0826 from Staphylococcus aureus. Acta Crystallogr F Struct Biol Commun, 70, 211-214. PubMed id: 24637759 DOI: 10.1107/S2053230X13034493

Date:

25-Jul-13 Release date: 18-Jun-14

Protein chain

A0A0H3JYD9  (A0A0H3JYD9_STAAM) -  N-acetyltransferase domain-containing protein from Staphylococcus aureus (strain Mu50 / ATCC 700699)

Seq: 164 a.a.

Struc: 156 a.a.

DOI no: 10.1107/S2053230X13034493

Acta Crystallogr F Struct Biol Commun 70:211-214 (2014)

PubMed id: 24637759

Purification, crystallization and preliminary X-ray diffraction analysis of the N-acetyltransferase SAV0826 from Staphylococcus aureus.

P.Srivastava, Y.B.Khandokar, J.K.Forwood.

ABSTRACT

Staphylococcus aureus is a prevalent microorganism that is capable of causing a wide range of infections and diseases. Several strains of this bacterial species have developed antibiotic resistance to methicillin and vancomycin, and higher death rates are still being reported each year owing to multidrug-resistant strains. Certain GCN5-related N-acetyltransferases (GNATs) exhibit a broad substrate range, including aminoglycosides, histones, other proteins and serotonin, and have been implicated in antibiotic drug resistance. Here, the expression, purification, crystallization and preliminary X-ray diffraction analysis of a GNAT from S. aureus (SaNAT) are reported. SaNAT was recombinantly expressed and crystallized by the hanging-drop vapour-diffusion method at 296 K, and the crystals diffracted to 1.7 Å resolution on the MX2 beamline at the Australian Synchrotron. The crystals belonged to space group P43212, with unit-cell parameters a = b = 84.86, c = 49.06 Å, α = β = γ = 90°. A single molecule is likely to be present in the asymmetric unit. A full structural and functional analysis is currently being undertaken to provide novel insights into the protein function, which in turn may provide a basis for drug design.