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PDBsum entry 2q83

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protein ligands Protein-protein interface(s) links
Transferase PDB id
2q83
Jmol
Contents
Protein chains
332 a.a. *
Ligands
ADN ×2
UNL ×2
EDO ×8
SO4 ×2
CIT
Waters ×187
* Residue conservation analysis
PDB id:
2q83
Name: Transferase
Title: Crystal structure of ytaa (2635576) from bacillus subtilis a resolution
Structure: Ytaa protein. Chain: a, b. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Strain: 168. Gene: ytaa, bsu30920. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.199     R-free:   0.210
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref: E.D.Scheeff et al. (2010). Genomics, evolution, and crystal structure of a new family of bacterial spore kinases. Proteins, 78, 1470-1482. PubMed id: 20077512
Date:
08-Jun-07     Release date:   26-Jun-07    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
O34656  (COTI_BACSU) -  Spore coat protein I
Seq:
Struc:
357 a.a.
332 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     spore wall   1 term 
  Biological process     metabolic process   2 terms 
  Biochemical function     transferase activity, transferring phosphorus-containing groups     1 term  

 

 
Proteins 78:1470-1482 (2010)
PubMed id: 20077512  
 
 
Genomics, evolution, and crystal structure of a new family of bacterial spore kinases.
E.D.Scheeff, H.L.Axelrod, M.D.Miller, H.J.Chiu, A.M.Deacon, I.A.Wilson, G.Manning.
 
  ABSTRACT  
 
Bacterial spore formation is a complex process of fundamental relevance to biology and human disease. The spore coat structure is complex and poorly understood, and the roles of many of the protein components remain unclear. We describe a new family of spore coat proteins, the bacterial spore kinases (BSKs), and the first crystal structure of a BSK, YtaA (CotI) from Bacillus subtilis. BSKs are widely distributed in spore-forming Bacillus and Clostridium species, and have a dynamic evolutionary history. Sequence and structure analyses indicate that the BSKs are CAKs, a prevalent group of small molecule kinases in bacteria that is distantly related to the eukaryotic protein kinases. YtaA has substantial structural similarity to CAKs, but also displays distinctive features that broaden our understanding of the CAK group. Evolutionary constraint analysis of the protein surfaces indicates that members of the BSK family have distinct clade-conserved patterns in the substrate binding region, and probably bind and phosphorylate distinct targets. Several classes of BSKs have apparently independently lost catalytic activity to become pseudokinases, indicating that the family also has a major noncatalytic function.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23202530 P.T.McKenney, A.Driks, and P.Eichenberger (2012).
The Bacillus subtilis endospore: assembly and functions of the multilayered coat.
  Nat Rev Microbiol, 11, 33-44.  
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.