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PDBsum entry 1mpx

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1mpx
Jmol
Contents
Protein chains
614 a.a. *
Ligands
GOL ×10
Metals
_CA ×4
Waters ×2246
* Residue conservation analysis
PDB id:
1mpx
Name: Hydrolase
Title: Alpha-amino acid ester hydrolase labeled with selenomethioni
Structure: Alpha-amino acid ester hydrolase. Chain: a, b, c, d. Engineered: yes
Source: Xanthomonas citri. Organism_taxid: 346. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
Resolution:
1.90Å     R-factor:   0.150     R-free:   0.178
Authors: T.R.M.Barends,J.J.Polderman-Tijmes,P.A.Jekel,C.M.H.Hensgens, Vries,D.B.Janssen,B.W.Dijkstra
Key ref:
T.R.Barends et al. (2003). The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases. J Biol Chem, 278, 23076-23084. PubMed id: 12684501 DOI: 10.1074/jbc.M302246200
Date:
13-Sep-02     Release date:   15-Apr-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q6YBS3  (Q6YBS3_XANCI) -  Alpha-amino acid ester hydrolase
Seq:
Struc:
 
Seq:
Struc:
637 a.a.
614 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.1.43  - Alpha-amino-acid esterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: An alpha-amino acid ester + H2O = an alpha-amino acid + an alcohol
alpha-amino acid ester
+ H(2)O
= alpha-amino acid
+ alcohol
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     hydrolase activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M302246200 J Biol Chem 278:23076-23084 (2003)
PubMed id: 12684501  
 
 
The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases.
T.R.Barends, J.J.Polderman-Tijmes, P.A.Jekel, C.M.Hensgens, E.J.de Vries, D.B.Janssen, B.W.Dijkstra.
 
  ABSTRACT  
 
alpha-Amino acid ester hydrolases (AEHs) catalyze the hydrolysis and synthesis of esters and amides with an alpha-amino group. As such, they can synthesize beta-lactam antibiotics from acyl compounds and beta-lactam nuclei obtained from the hydrolysis of natural antibiotics. This article describes the gene sequence and the 1.9-A resolution crystal structure of the AEH from Xanthomonas citri. The enzyme consists of an alpha/beta-hydrolase fold domain, a helical cap domain, and a jellyroll beta-domain. Structural homology was observed to the Rhodococcus cocaine esterase, indicating that both enzymes belong to the same class of bacterial hydrolases. Docking of a beta-lactam antibiotic in the active site explains the substrate specificity, specifically the necessity of an alpha-amino group on the substrate, and explains the low specificity toward the beta-lactam nucleus.
 
  Selected figure(s)  
 
Figure 3.
FIG. 3. A, stereo representation of the X. citri AEH tetramer, looking through the large entrance into the central cavity. Each monomer is individually colored. The figure was prepared using Molscript (45). B, stereo representation of the X. citri AEH monomer. The / -hydrolase fold domain is colored green, the cap domain orange, and the C-terminal jellyroll domain blue. The catalytic Ser-174 is shown in ball-and-stick representation. The figure was prepared using Molscript (45).
Figure 5.
FIG. 5. Stereo figure of the calcium binding motif. The coordinating residues are indicated. The figure was prepared using Bobscript (46) and Raster3D (47).
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 23076-23084) copyright 2003.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18305979 W.C.Lima, and C.F.Menck (2008).
Replacement of the arginine biosynthesis operon in Xanthomonadales by lateral gene transfer.
  J Mol Evol, 66, 266-275.  
17337538 G.Rivera-Cancel, D.Bocioaga, and A.G.Hay (2007).
Bacterial degradation of N,N-diethyl-m-toluamide (DEET): cloning and heterologous expression of DEET hydrolase.
  Appl Environ Microbiol, 73, 3105-3108.  
16672512 C.Elend, C.Schmeisser, C.Leggewie, P.Babiak, J.D.Carballeira, H.L.Steele, J.L.Reymond, K.E.Jaeger, and W.R.Streit (2006).
Isolation and biochemical characterization of two novel metagenome-derived esterases.
  Appl Environ Microbiol, 72, 3637-3645.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.