› 2z2p

X-ray diffraction
2.8Å resolution

Crystal Structure of catalytically inactive H270A virginiamycin B lyase from Staphylococcus aureus with Quinupristin

Released:
DOI: 10.2210/pdb2z2p/pdb
PDB entry 2z2p coloured by chain, front view.
PDB entry 2z2p coloured by chain, side view.
PDB entry 2z2p coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis for streptogramin B resistance in Staphylococcus aureus by virginiamycin B lyase.
Korczynska M, Mukhtar TA, Wright GD, Berghuis AM
Proc Natl Acad Sci U S A 104 10388-93 (2007)
PMID: 17563376

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148231 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Virginiamycin B lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 299 amino acids
Theoretical weight: 33.03 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P17978 (Residues: 1-299; Coverage: 100%)
Gene names: vgb, vgh
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Quinupristin Chains: C, D
Molecule details ›
Chains: C, D
Length: 8 amino acids
Theoretical weight: 1.02 KDa
Source organism: Streptomyces graminofaciens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand DOL 2 x DOL
1 modified residue:
Ligand MHU 2 x MHU

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 70.999Å b: 93.7Å c: 95.301Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.268 0.262 0.318
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

10 review citations

The rise of the Enterococcus: beyond vancomycin resistance.
Arias et al. (2012)
9 more

4 mentions without citation

Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases.
Fieldhouse et al. (2010)
3 more