4QLO

Crystal Structure of homoserine o-acetyltransferase from Staphylococcus aureus

PDB DOI: https://doi.org/10.2210/pdb4QLO/pdb

Classification: TRANSFERASE
Organism(s): Staphylococcus aureus subsp. aureus USA300_TCH1516
Expression System: Escherichia coli BL21
Mutation(s): No

Deposited: 2014-06-12 Released: 2014-08-20
Deposition Author(s): Thangavelu, B., Pavlovsky, A.G., Viola, R.E.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.45 Å
R-Value Free: 0.291
R-Value Work: 0.240
R-Value Observed: 0.242

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Structure of homoserine O-acetyltransferase from Staphylococcus aureus: the first Gram-positive ortholog structure.

Thangavelu, B., Pavlovsky, A.G., Viola, R.

(2014) Acta Crystallogr Sect F Struct Biol Cryst Commun 70: 1340-1345

PubMed: 25286936 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1107/S2053230X14018664
Primary Citation of Related Structures:
4QLO

PubMed Abstract:
Homoserine O-acetyltransferase (HTA) catalyzes the formation of L-O-acetyl-homoserine from L-homoserine through the transfer of an acetyl group from acetyl-CoA. This is the first committed step required for the biosynthesis of methionine in many fungi, Gram-positive bacteria and some Gram-negative bacteria. The structure of HTA from Staphylococcus aureus (SaHTA) has been determined to a resolution of 2.45 Å. The structure belongs to the α/β-hydrolase superfamily, consisting of two distinct domains: a core α/β-domain containing the catalytic site and a lid domain assembled into a helical bundle. The active site consists of a classical catalytic triad located at the end of a deep tunnel. Structure analysis revealed some important differences for SaHTA compared with the few known structures of HTA.

Organizational Affiliation

Department of Chemistry and Biochemistry, The University of Toledo, Toledo, OH 43606, USA.

Macromolecule Content

Total Structure Weight: 41.24 kDa
Atom Count: 2,688
Modelled Residue Count: 327
Deposited Residue Count: 360
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
homoserine O-acetyltransferase	A	360	Staphylococcus aureus subsp. aureus USA300_TCH1516	Mutation(s): 0 Gene Names: AZ30_00060, metX, SACOL0012, USA300HOU_0012 EC: 2.3.1.31
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.45 Å
R-Value Free: 0.291
R-Value Work: 0.240
R-Value Observed: 0.242
Space Group: P 6₁ 2 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 49.155	α = 90
b = 49.155	β = 90
c = 481.417	γ = 120

Software Package:

Software Name	Purpose
CrystalClear	data collection
BALBES	phasing
REFMAC	refinement
HKL-2000	data reduction
HKL-2000	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2014-08-20

Deposition Author(s):

Pavlovsky, A.G.

Revision History (Full details and data files)

Version 1.0: 2014-08-20
Type: Initial release
Version 1.1: 2014-12-17
Changes: Database references
Version 1.2: 2024-02-28
Changes: Data collection, Database references

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.