3N0S

Crystal structure of BA2930 mutant (H183A) in complex with AcCoA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.15 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.176 

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Ligand Structure Quality Assessment 


This is version 1.5 of the entry. See complete history


Literature

Structural Analysis of a Putative Aminoglycoside N-Acetyltransferase from Bacillus anthracis.

Klimecka, M.M.Chruszcz, M.Font, J.Skarina, T.Shumilin, I.Onopryienko, O.Porebski, P.J.Cymborowski, M.Zimmerman, M.D.Hasseman, J.Glomski, I.J.Lebioda, L.Savchenko, A.Edwards, A.Minor, W.

(2011) J Mol Biol 410: 411-423

  • DOI: https://doi.org/10.1016/j.jmb.2011.04.076
  • Primary Citation of Related Structures:  
    3E4F, 3IJW, 3KZL, 3N0M, 3N0S

  • PubMed Abstract: 

    For the last decade, worldwide efforts for the treatment of anthrax infection have focused on developing effective vaccines. Patients that are already infected are still treated traditionally using different types of standard antimicrobial agents. The most popular are antibiotics such as tetracyclines and fluoroquinolones. While aminoglycosides appear to be less effective antimicrobial agents than other antibiotics, synthetic aminoglycosides have been shown to act as potent inhibitors of anthrax lethal factor and may have potential application as antitoxins. Here, we present a structural analysis of the BA2930 protein, a putative aminoglycoside acetyltransferase, which may be a component of the bacterium's aminoglycoside resistance mechanism. The determined structures revealed details of a fold characteristic only for one other protein structure in the Protein Data Bank, namely, YokD from Bacillus subtilis. Both BA2930 and YokD are members of the Antibiotic_NAT superfamily (PF02522). Sequential and structural analyses showed that residues conserved throughout the Antibiotic_NAT superfamily are responsible for the binding of the cofactor acetyl coenzyme A. The interaction of BA2930 with cofactors was characterized by both crystallographic and binding studies.


  • Organizational Affiliation

    Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Aminoglycoside N3-acetyltransferaseA,
B [auth D],
C,
D [auth B]
268Bacillus anthracis str. AmesMutation(s): 1 
Gene Names: aacC7BA_2930GBAA2930GBAA_2930
EC: 2.3.1.81
UniProt
Find proteins for A0A3P1UCA6 (Bacillus anthracis)
Explore A0A3P1UCA6 
Go to UniProtKB:  A0A3P1UCA6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A3P1UCA6
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A,
B [auth D],
C,
D [auth B]
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Binding Affinity Annotations 
IDSourceBinding Affinity
ACO Binding MOAD:  3N0S Kd: 3720 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 72.036α = 90
b = 109.441β = 111.86
c = 74.048γ = 90
Software Package:
Software NamePurpose
MAR345dtbdata collection
HKL-3000phasing
MOLREPphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2010-06-09
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2011-08-03
    Changes: Database references
  • Version 1.3: 2022-04-13
    Changes: Database references, Derived calculations, Structure summary
  • Version 1.4: 2023-09-06
    Changes: Data collection, Refinement description
  • Version 1.5: 2023-11-22
    Changes: Data collection