4LUA

Crystal structure of N-acetyltransferase from Staphylococcus aureus Mu50

4LUA の概要

• エントリーDOI: 10.2210/pdb4lua/pdb
• 関連するPDBエントリー: 4MBU
• 分子名称: N-acetyltransferase, GLYCEROL (3 entities in total)
• 機能のキーワード: nat_sf, acetyltransferase, transferase
• 由来する生物種: Staphylococcus aureus subsp. aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19344.64

構造登録者

Srivastava, P.,Forwood, J.K. (登録日: 2013-07-25, 公開日: 2014-06-18, 最終更新日: 2023-09-20)

主引用文献

Srivastava, P.,Khandokar, Y.B.,Forwood, J.K.
Purification, crystallization and preliminary X-ray diffraction analysis of the N-acetyltransferase SAV0826 from Staphylococcus aureus.
Acta Crystallogr.,Sect.F, 70:211-214, 2014

PubMed 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.

PubMed: 24637759
DOI: 10.1107/S2053230X13034493

実験手法

X-RAY DIFFRACTION (1.6001 Å)