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Hydrolase PDB id
2j13
Jmol
Contents
Protein chain
207 a.a. *
Ligands
ACT ×2
CAC
Metals
_ZN ×4
Waters ×179
* Residue conservation analysis
PDB id:
2j13
Name: Hydrolase
Title: Structure of a family 4 carbohydrate esterase from bacillus anthracis
Structure: Polysaccharide deacetylase. Chain: a. Synonym: carbohydrate esterase. Engineered: yes
Source: Bacillus anthracis. Organism_taxid: 198094. Strain: ames. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.7Å     R-factor:   0.188     R-free:   0.230
Authors: T.M.Gloster,L.Oberbarnscheidt,E.J.Taylor,G.J.Davies
Key ref:
L.Oberbarnscheidt et al. (2007). Structure of a carbohydrate esterase from Bacillus anthracis. Proteins, 66, 250-252. PubMed id: 17063474 DOI: 10.1002/prot.21217
Date:
08-Aug-06     Release date:   03-Oct-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q81Z49  (Q81Z49_BACAN) -  Delta-lactam-biosynthetic de-N-acetylase
Seq:
Struc: 		260 a.a.
207 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     catalytic activity     3 terms  

 

 
DOI no: 10.1002/prot.21217 Proteins 66:250-252 (2007)
PubMed id: 17063474  
 
 
Structure of a carbohydrate esterase from Bacillus anthracis.
L.Oberbarnscheidt, E.J.Taylor, G.J.Davies, T.M.Gloster.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. (A) Ribbon representation of BaCE4, color-ramped from N- (blue) to C- (red) terminus. Acetate and cacodylate ions are shown in ball-and-stick representation, and zinc ions are shown as spheres. (B) Active site of BaCE4, which shows a zinc ion (sphere) coordinating a cacodylate ion and an acetate ion that were all sequestered from the crystallization mother liquor, and His103 and His107. Observed electron density for the maximum likelihood weighted 2F[obs] - F[calc] map is contoured at 1.5 (0.36e Å^-3). (C) Proposed mechanism for CE4 polysaccharide deacetylation. Asp52 acts as a base by activating the nucleophilic water residue and His 201 acts as an acid to aid leaving group departure. The reaction passes through a tetrahedral transition state, which is mimicked here by the cacodylate ion.
 
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 66, 250-252) copyright 2007.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18550550 I.Ramazzina, L.Cendron, C.Folli, R.Berni, D.Monteverdi, G.Zanotti, and R.Percudani (2008).
Logical Identification of an Allantoinase Analog (puuE) Recruited from Polysaccharide Deacetylases.
  J Biol Chem, 283, 23295-23304.
PDB codes: 3cl6 3cl7 3cl8
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