2PL2

Crystal structure of TTC0263: a thermophilic TPR protein in Thermus thermophilus HB27

Summary for 2PL2

• Entry DOI: 10.2210/pdb2pl2/pdb
• Descriptor: Hypothetical conserved protein TTC0263 (2 entities in total)
• Functional Keywords: tpr, protein binding
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 48777.79

Authors

Lim, H.,Kim, K.,Han, D.,Oh, J. (deposition date: 2007-04-18, release date: 2008-03-04, Last modification date: 2024-03-13)

Primary citation

Lim, H.,Kim, K.,Han, D.,Oh, J.,Kim, Y.
Crystal structure of TTC0263, a thermophilic TPR protein from Thermus thermophilus HB27.
Mol.Cell, 24:27-36, 2007

PubMed Abstract: 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.

PubMed: 17846496

Experimental method

X-RAY DIFFRACTION (2.5 Å)