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 
  • R-Value Observed: 0.167 

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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.

(2020) Protein Sci 29: 1035-1039

  • DOI: https://doi.org/10.1002/pro.3808
  • Primary Citation of Related Structures:  
    6P2T, 6ULL

  • 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 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.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
N-acetyl-alpha-D-glucosaminyl L-malate deacetylase 1256Bacillus subtilis subsp. subtilis str. 168Mutation(s): 0 
Gene Names: bshB1, jojG, ypjG, BSU22470
EC: 3.5.1
UniProt
Find proteins for P42981 (Bacillus subtilis (strain 168))
Explore P42981 
Go to UniProtKB:  P42981
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP42981
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.197 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.167 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 99.539α = 90
b = 99.539β = 90
c = 184.87γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
Aimlessdata scaling
PDB_EXTRACTdata extraction
XDSdata reduction
PHASERphasing

Structure Validation

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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  (Full details and data files)

  • Version 1.0: 2020-01-08
    Type: Initial release
  • Version 1.1: 2020-04-08
    Changes: Database references
  • Version 1.2: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Data collection, Derived calculations
  • Version 1.3: 2023-10-11
    Changes: Data collection, Database references, Refinement description, Structure summary