spacer
spacer

PDBsum entry 3h4l

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
DNA binding protein, protein binding PDB id
3h4l
Jmol
Contents
Protein chains
333 a.a. *
Ligands
ANP ×2
Metals
_MG ×2
Waters ×141
* Residue conservation analysis
PDB id:
3h4l
Name: DNA binding protein, protein binding
Title: Crystal structure of n terminal domain of a DNA repair prote
Structure: DNA mismatch repair protein pms1. Chain: a, b. Fragment: unp residues 1-365. Synonym: postmeiotic segregation protein 1. Engineered: yes
Source: Saccharomyces cerevisiae. Brewer's yeast,lager beer yeast,yeast. Organism_taxid: 4932. Gene: pms1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.235     R-free:   0.286
Authors: M.E.Arana,S.F.Holmes,J.M.Fortune,A.F.Moon,L.C.Pedersen,T.A.K
Key ref: M.E.Arana et al. (2010). Functional residues on the surface of the N-terminal domain of yeast Pms1. DNA Repair (Amst), 9, 448-457. PubMed id: 20138591
Date:
20-Apr-09     Release date:   02-Mar-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P14242  (PMS1_YEAST) -  DNA mismatch repair protein PMS1
Seq:
Struc:
 
Seq:
Struc:
873 a.a.
333 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     mismatch repair complex   1 term 
  Biological process     mismatch repair   1 term 
  Biochemical function     ATP binding     2 terms  

 

 
DNA Repair (Amst) 9:448-457 (2010)
PubMed id: 20138591  
 
 
Functional residues on the surface of the N-terminal domain of yeast Pms1.
M.E.Arana, S.F.Holmes, J.M.Fortune, A.F.Moon, L.C.Pedersen, T.A.Kunkel.
 
  ABSTRACT  
 
Saccharomyces cerevisiae MutLalpha is a heterodimer of Mlh1 and Pms1 that participates in DNA mismatch repair (MMR). Both proteins have weakly conserved C-terminal regions (CTDs), with the CTD of Pms1 harboring an essential endonuclease activity. These proteins also have conserved N-terminal domains (NTDs) that bind and hydrolyze ATP and bind to DNA. To better understand Pms1 functions and potential interactions with DNA and/or other proteins, we solved the 2.5A crystal structure of yeast Pms1 (yPms1) NTD. The structure is similar to the homologous NTDs of Escherichia coli MutL and human PMS2, including the site involved in ATP binding and hydrolysis. The structure reveals a number of conserved, positively charged surface residues that do not interact with other residues in the NTD and are therefore candidates for interactions with DNA, with the CTD and/or with other proteins. When these were replaced with glutamate, several replacements resulted in yeast strains with elevated mutation rates. Two replacements also resulted in NTDs with decreased DNA binding affinity in vitro, suggesting that these residues contribute to DNA binding that is important for mismatch repair. Elevated mutation rates also resulted from surface residue replacements that did not affect DNA binding, suggesting that these conserved residues serve other functions, possibly involving interactions with other MMR proteins.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21354867 A.N.Schorzman, L.Perera, J.M.Cutalo-Patterson, L.C.Pedersen, L.G.Pedersen, T.A.Kunkel, and K.B.Tomer (2011).
Modeling of the DNA-binding site of yeast Pms1 by mass spectrometry.
  DNA Repair (Amst), 10, 454-465.  
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.