PDBsum entry 2pl2

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protein Protein-protein interface(s) links
Protein binding PDB id
Jmol PyMol
Protein chains
194 a.a. *
Waters ×56
* Residue conservation analysis
PDB id:
Name: Protein binding
Title: Crystal structure of ttc0263: a thermophilic tpr protein in thermophilus hb27
Structure: Hypothetical conserved protein ttc0263. Chain: a, b. Fragment: residues 25-241. Engineered: yes
Source: Thermus thermophilus. Organism_taxid: 262724. Strain: hb27. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.50Å     R-factor:   0.236    
Authors: H.Lim,K.Kim,D.Han,J.Oh
Key ref: H.Lim et al. (2007). Crystal structure of TTC0263, a thermophilic TPR protein from Thermus thermophilus HB27. Mol Cells, 24, 27-36. PubMed id: 17846496
18-Apr-07     Release date:   04-Mar-08    
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Protein chains
Pfam   ArchSchema ?
Q72L02  (Q72L02_THET2) -  Hypothetical conserved protein
355 a.a.
194 a.a.
Key:    PfamA domain  Secondary structure  CATH domain


Mol Cells 24:27-36 (2007)
PubMed id: 17846496  
Crystal structure of TTC0263, a thermophilic TPR protein from Thermus thermophilus HB27.
H.Lim, K.Kim, D.Han, J.Oh, Y.Kim.
The hypothetical protein TTC0263 of Thermus thermophilus HB27 is a thermophilic tetratricopeptide repeat (TPR)-containing protein. In the present study, the TPR region (residues 26-230) was resolved at 2.5 A with R-factors of R/Rfree = 23.6%/28.6%. TTC0263 consists of 11 helices that form five TPR units. Uniquely, it contains one atypical "extended" TPR (eTPR) unit. This comprises extended helical residues near the loop region of TTC0263, such that the helical length of eTPR is longer than that of the canonical TPR sequence. In addition, the hybrid TPR domain of TTC0263 possesses oligomer-forming characteristics. TPR domains are generally involved in forming multi-subunit complexes by interacting with each other or with other subunit proteins. The dynamic structure of TTC0263 described here goes some way to explaining how TPR domains mediate the formation of multi-subunit complexes.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18606795 S.Park, and R.L.Ely (2008).
Candidate stress genes of Nitrosomonas europaea for monitoring inhibition of nitrification by heavy metals.
  Appl Environ Microbiol, 74, 5475-5482.  
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