Crystal structure of TTC0263, a thermophilic TPR protein from Thermus thermophilus HB27
- PMID: 17846496
Crystal structure of TTC0263, a thermophilic TPR protein from Thermus thermophilus HB27
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.
Similar articles
-
Expression, crystallization and preliminary X-ray analysis of an outer membrane protein from Thermus thermophilus HB27.Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt 6):533-6. doi: 10.1107/S1744309108013602. Epub 2008 May 23. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008. PMID: 18540069 Free PMC article.
-
Crystal structure of a conserved hypothetical protein TT1751 from Thermus thermophilus HB8.Proteins. 2004 Dec 1;57(4):883-7. doi: 10.1002/prot.20282. Proteins. 2004. PMID: 15481054 No abstract available.
-
Crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 reveals a new protein family with an RNA recognition motif-like domain.Protein Sci. 2006 Jun;15(6):1494-9. doi: 10.1110/ps.062131106. Epub 2006 May 2. Protein Sci. 2006. PMID: 16672237 Free PMC article.
-
Versatile TPR domains accommodate different modes of target protein recognition and function.Cell Stress Chaperones. 2011 Jul;16(4):353-67. doi: 10.1007/s12192-010-0248-0. Epub 2010 Dec 9. Cell Stress Chaperones. 2011. PMID: 21153002 Free PMC article. Review.
-
Ribosomal proteins from Thermus thermophilus for structural investigations.Biochimie. 1992 Apr;74(4):327-36. doi: 10.1016/0300-9084(92)90110-z. Biochimie. 1992. PMID: 1637860 Review.
Cited by
-
Self-recognition mechanism of MamA, a magnetosome-associated TPR-containing protein, promotes complex assembly.Proc Natl Acad Sci U S A. 2011 Aug 16;108(33):E480-7. doi: 10.1073/pnas.1103367108. Epub 2011 Jul 22. Proc Natl Acad Sci U S A. 2011. PMID: 21784982 Free PMC article.
-
Crystallization and preliminary crystallographic analysis of the Magnetospirillum magneticum AMB-1 and M. gryphiswaldense MSR-1 magnetosome-associated proteins MamA.Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jul 1;66(Pt 7):824-7. doi: 10.1107/S1744309110018300. Epub 2010 Jun 24. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010. PMID: 20606283 Free PMC article.
-
Phospholipid transfer function of PTPIP51 at mitochondria-associated ER membranes.EMBO Rep. 2021 Jun 4;22(6):e51323. doi: 10.15252/embr.202051323. Epub 2021 May 2. EMBO Rep. 2021. PMID: 33938112 Free PMC article.
-
Candidate stress genes of Nitrosomonas europaea for monitoring inhibition of nitrification by heavy metals.Appl Environ Microbiol. 2008 Sep;74(17):5475-82. doi: 10.1128/AEM.00500-08. Epub 2008 Jul 7. Appl Environ Microbiol. 2008. PMID: 18606795 Free PMC article.
-
Structural, bioinformatic, and in vivo analyses of two Treponema pallidum lipoproteins reveal a unique TRAP transporter.J Mol Biol. 2012 Mar 9;416(5):678-96. doi: 10.1016/j.jmb.2012.01.015. Epub 2012 Jan 27. J Mol Biol. 2012. PMID: 22306465 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
