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PDBsum entry 3lwt

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protein links
Hydrolase PDB id
3lwt
Jmol
Contents
Protein chain
457 a.a. *
Waters ×168
* Residue conservation analysis
PDB id:
3lwt
Name: Hydrolase
Title: Crystal structure of the yeast sac1: implications for its phosphoinositide phosphatase function
Structure: Phosphoinositide phosphatase sac1. Chain: x. Fragment: cytosolic portion of yeast sac1. Synonym: recessive suppressor of secretory defect. Engineered: yes
Source: Saccharomyces cerevisiae. Brewer's yeast,lager beer yeast,yeast. Organism_taxid: 4932. Gene: rsd1, sac1, ykl212w. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.96Å     R-factor:   0.201     R-free:   0.243
Authors: Y.Mao,A.Manford,T.Xia,A.K.Saxena,C.Stefan,F.Hu,S.D.Emr
Key ref: A.Manford et al. (2010). Crystal structure of the yeast Sac1: implications for its phosphoinositide phosphatase function. EMBO J, 29, 1489-1498. PubMed id: 20389282
Date:
24-Feb-10     Release date:   05-May-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P32368  (SAC1_YEAST) -  Phosphoinositide phosphatase SAC1
Seq:
Struc:
 
Seq:
Struc:
623 a.a.
457 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     phosphoric ester hydrolase activity     1 term  

 

 
EMBO J 29:1489-1498 (2010)
PubMed id: 20389282  
 
 
Crystal structure of the yeast Sac1: implications for its phosphoinositide phosphatase function.
A.Manford, T.Xia, A.K.Saxena, C.Stefan, F.Hu, S.D.Emr, Y.Mao.
 
  ABSTRACT  
 
Sac family phosphoinositide (PI) phosphatases are an essential family of CX(5)R(T/S)-based enzymes, involved in numerous aspects of cellular function such as PI homeostasis, cellular signalling, and membrane trafficking. Genetic deletions of several Sac family members result in lethality in animal models and mutations of the Sac3 gene have been found in human hereditary diseases. In this study, we report the crystal structure of a founding member of this family, the Sac phosphatase domain of yeast Sac1. The 2.0 A resolution structure shows that the Sac domain comprises of two closely packed sub-domains, a novel N-terminal sub-domain and the PI phosphatase catalytic sub-domain. The structure further shows a striking conformation of the catalytic P-loop and a large positively charged groove at the catalytic site. These findings suggest an unusual mechanism for its dephosphorylation function. Homology structural modeling of human Fig4/Sac3 allows the mapping of several disease-related mutations and provides a framework for the understanding of the molecular mechanisms of human diseases.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21295699 C.J.Stefan, A.G.Manford, D.Baird, J.Yamada-Hanff, Y.Mao, and S.D.Emr (2011).
Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites.
  Cell, 144, 389-401.  
21145456 M.R.Wenk (2010).
Lipidomics: new tools and applications.
  Cell, 143, 888-895.  
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