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PDBsum entry 1t6s

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protein ligands Protein-protein interface(s) links
Structural genomics, unknown function PDB id
1t6s
Jmol
Contents
Protein chains
162 a.a. *
Ligands
NO3 ×21
Waters ×98
* Residue conservation analysis
PDB id:
1t6s
Name: Structural genomics, unknown function
Title: Crystal structure of a conserved hypothetical protein from c tepidum
Structure: Conserved hypothetical protein. Chain: a, b. Engineered: yes
Source: Chlorobium tepidum tls. Organism_taxid: 194439. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
Resolution:
1.95Å     R-factor:   0.216     R-free:   0.253
Authors: J.S.Kim,D.H.Shin,R.Kim,S.H.Kim,Berkeley Structural Genomics (Bsgc)
Key ref: J.S.Kim et al. (2006). Crystal structure of ScpB from Chlorobium tepidum, a protein involved in chromosome partitioning. Proteins, 62, 322-328. PubMed id: 16294331
Date:
07-May-04     Release date:   07-Dec-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8KF54  (Q8KF54_CHLTE) -  Segregation and condensation protein B
Seq:
Struc:
209 a.a.
162 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     chromosome separation   1 term 

 

 
Proteins 62:322-328 (2006)
PubMed id: 16294331  
 
 
Crystal structure of ScpB from Chlorobium tepidum, a protein involved in chromosome partitioning.
J.S.Kim, D.H.Shin, R.Pufan, C.Huang, H.Yokota, R.Kim, S.H.Kim.
 
  ABSTRACT  
 
Structural maintenance of chromosome (SMC) proteins are essential in chromosome condensation and interact with non-SMC proteins in eukaryotes and with segregation and condensation proteins (ScpA and ScpB) in prokaryotes. The highly conserved gene in Chlorobium tepidum gi 21646405 encodes ScpB (ScpB_ChTe). The high resolution crystal structure of ScpB_ChTe shows that the monomeric structure consists of two similarly shaped globular domains composed of three helices sided by beta-strands [a winged helix-turn-helix (HTH)], a motif observed in the C-terminal domain of Scc1, a functionally related eukaryotic ScpA homolog, as well as in many DNA binding proteins.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20305267 I.Callebaut, and J.P.Mornon (2010).
LOTUS, a new domain associated with small RNA pathways in the germline.
  Bioinformatics, 26, 1140-1144.  
19884503 A.D.Gelinas, M.Paschini, F.E.Reyes, A.Héroux, R.T.Batey, V.Lundblad, and D.S.Wuttke (2009).
Telomere capping proteins are structurally related to RPA with an additional telomere-specific domain.
  Proc Natl Acad Sci U S A, 106, 19298-19303.
PDB codes: 3k0x 3k10
18300244 J.S.Kim, S.Lee, B.S.Kang, M.H.Kim, H.S.Lee, and K.J.Kim (2008).
Crystal structure and domain characterization of ScpB from Mycobacterium tuberculosis.
  Proteins, 71, 1553-1556.
PDB code: 2z99
17764033 D.H.Shin, J.Hou, J.M.Chandonia, D.Das, I.G.Choi, R.Kim, and S.H.Kim (2007).
Structure-based inference of molecular functions of proteins of unknown function from Berkeley Structural Genomics Center.
  J Struct Funct Genomics, 8, 99.  
17355972 M.Gloyd, R.Ghirlando, L.A.Matthews, and A.Guarné (2007).
MukE and MukF form two distinct high affinity complexes.
  J Biol Chem, 282, 14373-14378.  
  18084093 S.Y.Kwon, B.S.Kang, M.H.Kim, and K.J.Kim (2007).
Cloning, expression, purification, crystallization and X-ray crystallographic analysis of ScpB (Rv1710) from Mycobacterium tuberculosis.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 1058-1060.  
16633335 T.Hirano (2006).
At the heart of the chromosome: SMC proteins in action.
  Nat Rev Mol Cell Biol, 7, 311-322.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.