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PDBsum entry 4fdg

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protein metals Protein-protein interface(s) links
Hydrolase PDB id
4fdg

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
592 a.a.
Metals
_ZN ×5
PDB id:
4fdg
Name: Hydrolase
Title: Crystal structure of an archaeal mcm filament
Structure: Minichromosome maintenance protein mcm. Chain: b, a, c, d, e. Fragment: unp residues 7-686. Engineered: yes
Source: Sulfolobus solfataricus. Organism_taxid: 2287. Strain: p2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
4.10Å     R-factor:   0.332     R-free:   0.341
Authors: I.M.Slaymaker,Y.Fu,A.B.Brewster,X.S.Chen
Key ref: I.M.Slaymaker et al. (2013). Mini-chromosome maintenance complexes form a filament to remodel DNA structure and topology. Nucleic Acids Res, 41, 3446-3456. PubMed id: 23361460 DOI: 10.1093/nar/gkt022
Date:
28-May-12     Release date:   06-Mar-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9UXG1  (MCM_SULSO) -  Minichromosome maintenance protein MCM from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Seq:
Struc:
 
Seq:
Struc:
686 a.a.
592 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.3.6.4.12  - Dna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
+ H2O
= ADP
+ phosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1093/nar/gkt022 Nucleic Acids Res 41:3446-3456 (2013)
PubMed id: 23361460  
 
 
Mini-chromosome maintenance complexes form a filament to remodel DNA structure and topology.
I.M.Slaymaker, Y.Fu, D.B.Toso, N.Ranatunga, A.Brewster, S.L.Forsburg, Z.H.Zhou, X.S.Chen.
 
  ABSTRACT  
 
Deregulation of mini-chromosome maintenance (MCM) proteins is associated with genomic instability and cancer. MCM complexes are recruited to replication origins for genome duplication. Paradoxically, MCM proteins are in excess than the number of origins and are associated with chromatin regions away from the origins during G1 and S phases. Here, we report an unusually wide left-handed filament structure for an archaeal MCM, as determined by X-ray and electron microscopy. The crystal structure reveals that an α-helix bundle formed between two neighboring subunits plays a critical role in filament formation. The filament has a remarkably strong electro-positive surface spiraling along the inner filament channel for DNA binding. We show that this MCM filament binding to DNA causes dramatic DNA topology change. This newly identified function of MCM to change DNA topology may imply a wider functional role for MCM in DNA metabolisms beyond helicase function. Finally, using yeast genetics, we show that the inter-subunit interactions, important for MCM filament formation, play a role for cell growth and survival.
 

 

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