3GJZ

Crystal structure of microcin immunity protein MccF from Bacillus anthracis str. Ames


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.189 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural and Functional Characterization of Microcin C Resistance Peptidase MccF from Bacillus anthracis.

Nocek, B.Tikhonov, A.Babnigg, G.Gu, M.Zhou, M.Makarova, K.S.Vondenhoff, G.Aerschot, A.V.Kwon, K.Anderson, W.F.Severinov, K.Joachimiak, A.

(2012) J Mol Biol 420: 366-383

  • DOI: https://doi.org/10.1016/j.jmb.2012.04.011
  • Primary Citation of Related Structures:  
    3GJZ, 3SR3, 3T5M, 3TYX, 3U1B

  • PubMed Abstract: 

    Microcin C (McC) is heptapeptide adenylate antibiotic produced by Escherichia coli strains carrying the mccABCDEF gene cluster encoding enzymes, in addition to the heptapeptide structural gene mccA, necessary for McC biosynthesis and self-immunity of the producing cell. The heptapeptide facilitates McC transport into susceptible cells, where it is processed releasing a non-hydrolyzable aminoacyl adenylate that inhibits an essential aminoacyl-tRNA synthetase. The self-immunity gene mccF encodes a specialized serine peptidase that cleaves an amide bond connecting the peptidyl or aminoacyl moieties of, respectively, intact and processed McC with the nucleotidyl moiety. Most mccF orthologs from organisms other than E. coli are not linked to the McC biosynthesis gene cluster. Here, we show that a protein product of one such gene, MccF from Bacillus anthracis (BaMccF), is able to cleave intact and processed McC, and we present a series of structures of this protein. Structural analysis of apo-BaMccF and its adenosine monophosphate complex reveals specific features of MccF-like peptidases that allow them to interact with substrates containing nucleotidyl moieties. Sequence analyses and phylogenetic reconstructions suggest that several distinct subfamilies form the MccF clade of the large S66 family of bacterial serine peptidases. We show that various representatives of the MccF clade can specifically detoxify non-hydrolyzable aminoacyl adenylates differing in their aminoacyl moieties. We hypothesize that bacterial mccF genes serve as a source of bacterial antibiotic resistance.


  • Organizational Affiliation

    Center for Structural Genomics of Infectious Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892-6612, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Microcin immunity protein MccF
A, B
336Bacillus anthracis str. AmesMutation(s): 0 
Gene Names: BAS1809BA_1949GBAA1949
UniProt
Find proteins for A0A6L8PEJ7 (Bacillus anthracis)
Explore A0A6L8PEJ7 
Go to UniProtKB:  A0A6L8PEJ7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A6L8PEJ7
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.189 
  • Space Group: P 43
  • Diffraction Data: https://doi.org/10.18430/M33GJZ
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 118.962α = 90
b = 118.962β = 90
c = 55.542γ = 90
Software Package:
Software NamePurpose
SBC-Collectdata collection
HKL-3000phasing
SHELXmodel building
MLPHAREphasing
DMmodel building
CCP4model building
ARP/wARPmodel building
Cootmodel building
REFMACrefinement
HKL-3000data reduction
HKL-3000data scaling
SHELXphasing
DMphasing
CCP4phasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-04-14
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2012-05-02
    Changes: Database references
  • Version 1.3: 2012-07-25
    Changes: Database references