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PDBsum entry 3p71

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protein ligands metals Protein-protein interface(s) links
Transferase/hydrolase PDB id
3p71
Jmol
Contents
Protein chains
315 a.a. *
303 a.a. *
Ligands
PEG
AN6
Metals
_MN ×2
Waters ×120
* Residue conservation analysis
PDB id:
3p71
Name: Transferase/hydrolase
Title: Crystal structure of the complex of lcmt-1 and pp2a
Structure: Leucine carboxyl methyltransferase 1. Chain: t. Synonym: protein-leucine o-methyltransferase. Engineered: yes. Mutation: yes. Serine/threonine-protein phosphatase 2a catalytic alpha isoform. Chain: c. Fragment: catalytic subunit alpha isoform.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: cgi-68, lcmt, lcmt1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: ppp2ca. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7101.
Resolution:
2.70Å     R-factor:   0.195     R-free:   0.249
Authors: Y.Xing,V.Stanevich,K.A.Satyshur,L Jiang
Key ref: V.Stanevich et al. (2011). The structural basis for tight control of PP2A methylation and function by LCMT-1. Mol Cell, 41, 331-342. PubMed id: 21292165
Date:
11-Oct-10     Release date:   16-Feb-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9UIC8  (LCMT1_HUMAN) -  Leucine carboxyl methyltransferase 1
Seq:
Struc:
334 a.a.
315 a.a.*
Protein chain
Pfam   ArchSchema ?
P67775  (PP2AA_HUMAN) -  Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Seq:
Struc:
309 a.a.
303 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: Chain C: E.C.3.1.3.16  - Protein-serine/threonine phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: [a protein]-serine/threonine phosphate + H2O = [a protein]- serine/threonine + phosphate
[a protein]-serine/threonine phosphate
+ H(2)O
= [a protein]- serine/threonine
+ phosphate
   Enzyme class 2: Chain T: E.C.2.1.1.233  - [Phosphatase 2A protein]-leucine-carboxy methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine = S-adenosyl- L-homocysteine + [phosphatase 2A protein]-leucine methyl ester
S-adenosyl-L-methionine
+ [phosphatase 2A protein]-leucine
=
S-adenosyl- L-homocysteine
Bound ligand (Het Group name = AN6)
matches with 50.00% similarity
+ [phosphatase 2A protein]-leucine methyl ester
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   13 terms 
  Biological process     positive regulation of protein serine/threonine kinase activity   39 terms 
  Biochemical function     protein binding     13 terms  

 

 
    reference    
 
 
Mol Cell 41:331-342 (2011)
PubMed id: 21292165  
 
 
The structural basis for tight control of PP2A methylation and function by LCMT-1.
V.Stanevich, L.Jiang, K.A.Satyshur, Y.Li, P.D.Jeffrey, Z.Li, P.Menden, M.F.Semmelhack, Y.Xing.
 
  ABSTRACT  
 
No abstract given.