6ULL

BshB from Bacillus subtilis complexed with a substrate analogue


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.197 
  • R-Value Work: 0.166 

wwPDB Validation 3D Report Full Report


This is version 1.0 of the entry. See complete history

Literature

X-ray crystallographic structure of BshB, the zinc-dependent deacetylase involved in bacillithiol biosynthesis.

Woodward, R.L.Castleman, M.M.Meloche, C.E.Karpen, M.E.Carlson, C.G.Yobi, W.H.Jepsen, J.C.Lewis, B.W.Zarnosky, B.N.Cook, P.D.

(2019) Protein Sci. --: --

  • DOI: 10.1002/pro.3808
  • Primary Citation of Related Structures:  

  • PubMed Abstract: 
  • Many gram-positive bacteria produce bacillithiol to aid in the maintenance of redox homeostasis and degradation of toxic compounds, including the antibiotic fosfomycin. Bacillithiol is produced via a three-enzyme pathway that includes the action of t ...

    Many gram-positive bacteria produce bacillithiol to aid in the maintenance of redox homeostasis and degradation of toxic compounds, including the antibiotic fosfomycin. Bacillithiol is produced via a three-enzyme pathway that includes the action of the zinc-dependent deacetylase BshB. Previous studies identified conserved aspartate and histidine residues within the active site that are involved in metal binding and catalysis, but the enzymatic mechanism is not fully understood. Here we report two X-ray crystallographic structures of BshB from Bacillus subtilis that provide insight into the BshB catalytic mechanism.


    Organizational Affiliation

    Department of Chemistry and Biochemistry, University of Mount Union, Alliance, Ohio.,Department of Chemistry, Grand Valley State University, Allendale, Michigan.




Macromolecules

Find similar proteins by: Sequence  |  Structure

Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
N-acetyl-alpha-D-glucosaminyl L-malate deacetylase 1
A
256Bacillus subtilis (strain 168)Mutation(s): 0 
Gene Names: bshB1 (jojG, ypjG)
EC: 3.5.1.-
Find proteins for P42981 (Bacillus subtilis (strain 168))
Go to UniProtKB:  P42981
Small Molecules
Ligands 3 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN

Download SDF File 
Download CCD File 
A
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
 Ligand Interaction
SO4
Query on SO4

Download SDF File 
Download CCD File 
A
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
 Ligand Interaction
RWI
Query on RWI

Download SDF File 
Download CCD File 
A
(2S)-2-({2-deoxy-2-[(hydroxycarbamoyl)amino]-alpha-D-glucopyranosyl}oxy)butanedioic acid
C11 H18 N2 O11
QOPUTRBEPJZLTE-NKQVSKEESA-N
 Ligand Interaction
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.197 
  • R-Value Work: 0.166 
  • Space Group: H 3 2
Unit Cell:
Length (Å)Angle (°)
a = 99.539α = 90.00
b = 99.539β = 90.00
c = 184.870γ = 120.00
Software Package:
Software NamePurpose
PDB_EXTRACTdata extraction
Aimlessdata scaling
XDSdata reduction
REFMACrefinement
PHASERphasing

Structure Validation

View Full Validation Report or Ramachandran Plots



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United States1R15GM117488

Revision History 

  • Version 1.0: 2020-01-08
    Type: Initial release