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PDBsum entry 3q9l

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protein ligands metals Protein-protein interface(s) links
Cell cycle, hydrolase PDB id
3q9l
Jmol
Contents
Protein chains
257 a.a. *
Ligands
ATP ×2
Metals
_MG ×2
Waters ×240
* Residue conservation analysis
PDB id:
3q9l
Name: Cell cycle, hydrolase
Title: The structure of the dimeric e.Coli mind-atp complex
Structure: Septum site-determining protein mind. Chain: a, b. Fragment: unp residues 1-260. Synonym: cell division inhibitor mind. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: mind. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.34Å     R-factor:   0.268     R-free:   0.307
Authors: W.Wu,K.-T.Park,J.Lutkenhaus,T.Holyoak
Key ref: W.Wu et al. (2011). Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC. Mol Microbiol, 79, 1515-1528. PubMed id: 21231967
Date:
08-Jan-11     Release date:   26-Jan-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0AEZ3  (MIND_ECOLI) -  Septum site-determining protein MinD
Seq:
Struc:
270 a.a.
257 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   2 terms 
  Biological process     cell cycle   5 terms 
  Biochemical function     nucleotide binding     4 terms  

 

 
Mol Microbiol 79:1515-1528 (2011)
PubMed id: 21231967  
 
 
Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.
W.Wu, K.T.Park, T.Holyoak, J.Lutkenhaus.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21545286 M.Loose, K.Kruse, and P.Schwille (2011).
Protein self-organization: lessons from the min system.
  Annu Rev Biophys, 40, 315-336.  
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.