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PDBsum entry 4je3

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protein Protein-protein interface(s) links
Cell cycle PDB id
4je3

 

 

 

 

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Contents
Protein chains
244 a.a.
77 a.a.
Waters ×136
PDB id:
4je3
Name: Cell cycle
Title: An iml3-chl4 heterodimer links the core centromere to factors required for accurate chromosome segregation
Structure: Central kinetochore subunit iml3. Chain: a. Synonym: increased minichromosome loss protein 3, minichromosome maintenance protein 19. Engineered: yes. Central kinetochore subunit chl4. Chain: b. Fragment: unp residues 361-458. Synonym: chromosome loss protein 4, chromosome transmission fidelity
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: iml3, mcm19, ybr107c, ybr0836. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: chl4, ctf17, mcm17, ydr254w, yd9320a.04. Expression_system_taxid: 562
Resolution:
2.28Å     R-factor:   0.186     R-free:   0.211
Authors: S.M.Hinshaw,S.C.Harrison
Key ref: S.M.Hinshaw and S.C.Harrison (2013). An Iml3-Chl4 heterodimer links the core centromere to factors required for accurate chromosome segregation. Cell Rep, 5, 29-36. PubMed id: 24075991 DOI: 10.1016/j.celrep.2013.08.036
Date:
26-Feb-13     Release date:   16-Oct-13    
PROCHECK
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 Headers
 References

Protein chain
P38265  (CENPL_YEAST) -  Inner kinetochore subunit IML3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
245 a.a.
244 a.a.
Protein chain
Pfam   ArchSchema ?
P38907  (CENPN_YEAST) -  Inner kinetochore subunit CHL4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
458 a.a.
77 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/j.celrep.2013.08.036 Cell Rep 5:29-36 (2013)
PubMed id: 24075991  
 
 
An Iml3-Chl4 heterodimer links the core centromere to factors required for accurate chromosome segregation.
S.M.Hinshaw, S.C.Harrison.
 
  ABSTRACT  
 
Accurate segregation of genetic material in eukaryotes relies on the kinetochore, a multiprotein complex that connects centromeric DNA with microtubules. In yeast and humans, two proteins-Mif2/CENP-C and Chl4/CNEP-N-interact with specialized centromeric nucleosomes and establish distinct but cross-connecting axes of chromatin-microtubule linkage. Proteins recruited by Chl4/CENP-N include a subset that regulates chromosome transmission fidelity. We show that Chl4 and a conserved member of this subset, Iml3, both from Saccharomyces cerevisiae, form a stable protein complex that interacts with Mif2 and Sgo1. We have determined the structures of an Iml3 homodimer and an Iml3-Chl4 heterodimer, which suggest a mechanism for regulating the assembly of this functional axis of the kinetochore. We propose that at the core centromere, the Chl4-Iml3 complex participates in recruiting factors, such as Sgo1, that influence sister chromatid cohesion and encourage sister kinetochore biorientation.
 

 

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