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PDBsum entry 2q0q

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2q0q
Jmol
Contents
Protein chains
(+ 2 more) 215 a.a. *
Ligands
SO4 ×8
GOL ×8
Waters ×1608
* Residue conservation analysis
PDB id:
2q0q
Name: Hydrolase
Title: Structure of the native m. Smegmatis aryl esterase
Structure: Aryl esterase. Chain: a, b, c, d, e, f, g, h. Engineered: yes
Source: Mycobacterium smegmatis. Organism_taxid: 1772. Strain: atcc19686. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.50Å     R-factor:   0.176     R-free:   0.196
Authors: I.I.Mathews,M.Soltis,M.Saldajeno,G.Ganshaw,R.Sala,W.Weyler, M.A.Cervin,G.Whited,R.Bott
Key ref: I.Mathews et al. (2007). Structure of a novel enzyme that catalyzes acyl transfer to alcohols in aqueous conditions. Biochemistry, 46, 8969-8979. PubMed id: 17636869 DOI: 10.1021/bi7002444
Date:
22-May-07     Release date:   11-Dec-07    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
A0R5U7  (A0R5U7_MYCS2) -  Lipolytic enzyme, G-D-S-L
Seq:
Struc:
216 a.a.
215 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     hydrolase activity     1 term  

 

 
DOI no: 10.1021/bi7002444 Biochemistry 46:8969-8979 (2007)
PubMed id: 17636869  
 
 
Structure of a novel enzyme that catalyzes acyl transfer to alcohols in aqueous conditions.
I.Mathews, M.Soltis, M.Saldajeno, G.Ganshaw, R.Sala, W.Weyler, M.A.Cervin, G.Whited, R.Bott.
 
  ABSTRACT  
 
The unusual architecture of the enzyme (MsAcT) isolated from Mycobacterium smegmatis forms the mechanistic basis for favoring alcoholysis over hydrolysis in water. Unlike hydrolases that perform alcoholysis only under anhydrous conditions, MsAcT demonstrates alcoholysis in substantially aqueous media and, in the presence of hydrogen peroxide, has a perhydrolysis:hydrolysis ratio 50-fold greater than that of the best lipase tested. The crystal structures of the apoenzyme and an inhibitor-bound form have been determined to 1.5 A resolution. MsAcT is an octamer in the asymmetric unit and forms a tightly associated aggregate in solution. Relative to other structurally similar monomers, MsAcT contains several insertions that contribute to the oligomerization and greatly restrict the shape of the active site, thereby limiting its accessibility. These properties create an environment by which MsAcT can catalyze transesterification reactions in an aqueous medium and suggests how a serine hydrolase can be engineered to be an efficient acyltransferase.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21069734 J.Ma, Q.Lu, Y.Yuan, H.Ge, K.Li, W.Zhao, Y.Gao, L.Niu, and M.Teng (2011).
Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae reveals a novel active site architecture and the basis of substrate specificity.
  Proteins, 79, 662-668.
PDB code: 3mil
19484411 S.Duncan, Q.Jing, A.Katona, R.J.Kazlauskas, J.Schilling, U.Tschirner, and W.W.Aldajani (2010).
Increased saccharification yields from aspen biomass upon treatment with enzymatically generated peracetic acid.
  Appl Biochem Biotechnol, 160, 1637-1652.  
19527641 S.Santini, J.M.Crowet, A.Thomas, M.Paquot, M.Vandenbol, P.Thonart, J.P.Wathelet, C.Blecker, G.Lognay, R.Brasseur, L.Lins, and B.Charloteaux (2009).
Study of Thermomyces lanuginosa lipase in the presence of tributyrylglycerol and water.
  Biophys J, 96, 4814-4825.  
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 code is shown on the right.