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PDBsum entry 1tqh

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protein ligands links
Hydrolase PDB id
1tqh
Jmol
Contents
Protein chain
242 a.a. *
Ligands
SO4 ×2
4PA
Waters ×153
* Residue conservation analysis
PDB id:
1tqh
Name: Hydrolase
Title: Covalent reaction intermediate revealed in crystal structure geobacillus stearothermophilus carboxylesterase est30
Structure: Carboxylesterase precursor. Chain: a. Engineered: yes
Source: Geobacillus stearothermophilus. Organism_taxid: 1422. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.63Å     R-factor:   0.171     R-free:   0.228
Authors: P.Liu,Y.F.Wang,H.E.Ewis,A.T.Abdelal,C.D.Lu,R.W.Harrison,I.T.
Key ref:
P.Liu et al. (2004). Covalent reaction intermediate revealed in crystal structure of the Geobacillus stearothermophilus carboxylesterase Est30. J Mol Biol, 342, 551-561. PubMed id: 15327954 DOI: 10.1016/j.jmb.2004.06.069
Date:
17-Jun-04     Release date:   28-Sep-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q06174  (EST_GEOSE) -  Carboxylesterase
Seq:
Struc:
246 a.a.
242 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.1.1  - Carboxylesterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A carboxylic ester + H2O = an alcohol + a carboxylate
carboxylic ester
+ H(2)O
= alcohol
+ carboxylate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     carboxylic ester hydrolase activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.jmb.2004.06.069 J Mol Biol 342:551-561 (2004)
PubMed id: 15327954  
 
 
Covalent reaction intermediate revealed in crystal structure of the Geobacillus stearothermophilus carboxylesterase Est30.
P.Liu, Y.F.Wang, H.E.Ewis, A.T.Abdelal, C.D.Lu, R.W.Harrison, I.T.Weber.
 
  ABSTRACT  
 
Est30 is a thermophilic carboxylesterase cloned from Geobacillus stearothermophilus that showed optimal hydrolysis of esters with short acyl chains at 70 degrees C. Est30 is a member of a new family of carboxylesterases with representatives in other Gram-positive bacteria. The crystal structure has been determined at 1.63A resolution using multiple anomalous dispersion data. The two-domain crystal structure showed a large domain with a modified alpha/beta hydrolase core including a seven, rather than an eight-stranded beta sheet, and a smaller cap domain comprising three alpha helices. The catalytic triad consists of residues Ser94, Asp193, and His223. A 100Da tetrahedral ligand was observed to be covalently bound to the side-chain of Ser94. The propyl acetate ligand represents the first tetrahedral intermediate in the reaction mechanism. Therefore, this Est30 crystal structure will help understand the mode of action of all enzymes in the serine hydrolase superfamily.
 
  Selected figure(s)  
 
Figure 2.
Figure 2. The active site region of Est30. (a) 2FoKFc electron density map contoured at 1.6s. (b) Inter- acting residues. Interatomic inter- actions are shown in broken lines with distances in Å . The negative charge of the oxygen atom of the tetrahedral intermediate and the NH groups of Leu95 and Phe25 form an oxyanion hole (labeled in red).
 
  The above figure is reprinted by permission from Elsevier: J Mol Biol (2004, 342, 551-561) copyright 2004.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20587647 D.M.Charbonneau, F.Meddeb-Mouelhi, and M.Beauregard (2010).
A novel thermostable carboxylesterase from Geobacillus thermodenitrificans: evidence for a new carboxylesterase family.
  J Biochem, 148, 299-308.  
20217440 R.Al Khudary, R.Venkatachalam, M.Katzer, S.Elleuche, and G.Antranikian (2010).
A cold-adapted esterase of a novel marine isolate, Pseudoalteromonas arctica: gene cloning, enzyme purification and characterization.
  Extremophiles, 14, 273-285.  
19304850 S.Montoro-García, I.Martínez-Martínez, J.Navarro-Fernández, H.Takami, F.García-Carmona, and A.Sánchez-Ferrer (2009).
Characterization of a novel thermostable carboxylesterase from Geobacillus kaustophilus HTA426 shows the existence of a new carboxylesterase family.
  J Bacteriol, 191, 3076-3085.  
18437283 D.de Pascale, A.M.Cusano, F.Autore, E.Parrilli, G.di Prisco, G.Marino, and M.L.Tutino (2008).
The cold-active Lip1 lipase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 is a member of a new bacterial lipolytic enzyme family.
  Extremophiles, 12, 311-323.  
17466017 M.Levisson, J.van der Oost, and S.W.Kengen (2007).
Characterization and structural modeling of a new type of thermostable esterase from Thermotoga maritima.
  FEBS J, 274, 2832-2842.  
17239398 P.Liu, H.E.Ewis, P.C.Tai, C.D.Lu, and I.T.Weber (2007).
Crystal structure of the Geobacillus stearothermophilus carboxylesterase Est55 and its activation of prodrug CPT-11.
  J Mol Biol, 367, 212-223.
PDB codes: 2ogs 2ogt
17428787 S.Lun, and W.R.Bishai (2007).
Characterization of a novel cell wall-anchored protein with carboxylesterase activity required for virulence in Mycobacterium tuberculosis.
  J Biol Chem, 282, 18348-18356.  
16639719 B.M.Liederer, and R.T.Borchardt (2006).
Enzymes involved in the bioconversion of ester-based prodrugs.
  J Pharm Sci, 95, 1177-1195.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.