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PDBsum entry 1zoi

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protein Protein-protein interface(s) links
Hydrolase PDB id
1zoi
Jmol
Contents
Protein chains
275 a.a. *
Waters ×317
* Residue conservation analysis
PDB id:
1zoi
Name: Hydrolase
Title: Crystal structure of a stereoselective esterase from pseudomonas putida ifo12996
Structure: Esterase. Chain: a, b, c. Engineered: yes
Source: Pseudomonas putida. Organism_taxid: 303. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Trimer (from PQS)
Resolution:
1.60Å     R-factor:   0.220     R-free:   0.239
Authors: F.Elmi,H.T.Lee,J.Y.Huang,Y.C.Hsieh,Y.L.Wang,Y.J.Chen, S.Y.Shaw,C.J.Chen
Key ref: F.Elmi et al. (2005). Stereoselective esterase from Pseudomonas putida IFO12996 reveals alpha/beta hydrolase folds for D-beta-acetylthioisobutyric acid synthesis. J Bacteriol, 187, 8470-8476. PubMed id: 16321951
Date:
13-May-05     Release date:   02-May-06    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q3HWU8  (Q3HWU8_PSEPU) -  Esterase
Seq:
Struc:
276 a.a.
275 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
J Bacteriol 187:8470-8476 (2005)
PubMed id: 16321951  
 
 
Stereoselective esterase from Pseudomonas putida IFO12996 reveals alpha/beta hydrolase folds for D-beta-acetylthioisobutyric acid synthesis.
F.Elmi, H.T.Lee, J.Y.Huang, Y.C.Hsieh, Y.L.Wang, Y.J.Chen, S.Y.Shaw, C.J.Chen.
 
  ABSTRACT  
 
Esterase (EST) from Pseudomonas putida IFO12996 catalyzes the stereoselective hydrolysis of methyl dl-beta-acetylthioisobutyrate (dl-MATI) to produce d-beta-acetylthioisobutyric acid (DAT), serving as a key intermediate for the synthesis of angiotensin-converting enzyme inhibitors. The EST gene was cloned and expressed in Escherichia coli; the recombinant protein is a non-disulfide-linked homotrimer with a monomer molecular weight of 33,000 in both solution and crystalline states, indicating that these ESTs function as trimers. EST hydrolyzed dl-MATI to produce DAT with a degree of conversion of 49.5% and an enantiomeric excess value of 97.2% at an optimum pH of about 8 to 10 and an optimum temperature of about 57 to 67 degrees C. The crystal structure of EST has been determined by X-ray diffraction to a resolution of 1.6 A, confirming that EST is a member of the alpha/beta hydrolase fold superfamily of enzymes and includes a catalytic triad of Ser97, Asp227, and His256. The active site is located approximately in the middle of the molecule at the end of a pocket approximately 12 A deep. EST can hydrolyze the methyl ester group without affecting the acetylthiol ester moiety in dl-MATI. The examination of substrate specificity of EST toward other linear esters revealed that the enzyme showed specific activity toward methyl esters and that it recognized the configuration at C-2.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23275166 A.Gao, G.Y.Mei, S.Liu, P.Wang, Q.Tang, Y.P.Liu, H.Wen, X.M.An, L.Q.Zhang, X.X.Yan, and D.C.Liang (2013).
High-resolution structures of AidH complexes provide insights into a novel catalytic mechanism for N-acyl homoserine lactonase.
  Acta Crystallogr D Biol Crystallogr, 69, 82-91.
PDB codes: 4g5x 4g8b 4g8c 4g8d 4g9e 4g9g
21247902 J.Hwang, Y.Kim, H.B.Kang, L.Jaroszewski, A.M.Deacon, H.Lee, W.C.Choi, K.J.Kim, C.H.Kim, B.S.Kang, J.O.Lee, T.K.Oh, J.W.Kim, I.A.Wilson, and M.H.Kim (2011).
Crystal structure of the human N-Myc downstream-regulated gene 2 protein provides insight into its role as a tumor suppressor.
  J Biol Chem, 286, 12450-12460.
PDB codes: 2qmq 2xmq 2xmr 2xms
19957260 G.Labar, C.Bauvois, F.Borel, J.L.Ferrer, J.Wouters, and D.M.Lambert (2010).
Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling.
  Chembiochem, 11, 218-227.
PDB code: 3hju
20099871 K.M.McCulloch, T.Mukherjee, T.P.Begley, and S.E.Ealick (2010).
Structure determination and characterization of the vitamin B6 degradative enzyme (E)-2-(acetamidomethylene)succinate hydrolase.
  Biochemistry, 49, 1226-1235.
PDB code: 3kxp
19184135 M.C.Hanna, and C.Blackstone (2009).
Interaction of the SPG21 protein ACP33/maspardin with the aldehyde dehydrogenase ALDH16A1.
  Neurogenetics, 10, 217-228.  
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.