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2cwq
From Proteopedia
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'''Crystal structure of conserved protein TTHA0727 from Thermus thermophilus HB8''' | '''Crystal structure of conserved protein TTHA0727 from Thermus thermophilus HB8''' | ||
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[[Category: Terada, T.]] | [[Category: Terada, T.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
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| - | [[Category: | + | [[Category: Conserved hypothetical protein]] |
| - | [[Category: | + | [[Category: National project on protein structural and functional analyse]] |
| - | [[Category: | + | [[Category: Nppsfa]] |
| - | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
| - | [[Category: | + | [[Category: Rsgi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:13:59 2008'' | |
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Revision as of 20:14, 3 May 2008
Crystal structure of conserved protein TTHA0727 from Thermus thermophilus HB8
Overview
TTHA0727 is a conserved hypothetical protein from Thermus thermophilus HB8, with a molecular mass of 12.6 kDa. TTHA0727 belongs to the carboxymuconolactone decarboxylase (CMD) family (Pfam 02627). A sequence comparison with its homologs suggested that TTHA0727 is a distinct protein from alkylhydroperoxidase AhpD and gamma-carboxymuconolactone decarboxylase in the CMD family. Here we report the 1.9 A crystal structure of TTHA0727 (PDB ID: 2CWQ) determined by the multiwavelength anomalous dispersion method. The TTHA0727 monomer structure consists of seven alpha-helices (alpha1-alpha7) and one short 3(10)-helix. The crystal structure and the analytical ultracentrifugation revealed that TTHA0727 forms a hexameric ring structure in solution. The electrostatic potential distribution on the solvent-accessible surface of the TTHA0727 hexamer showed that positively charged regions exist on the side of the ring structure, suggesting that TTHA0727 interacts with some negatively charged molecules. A structural homology search revealed that the structure of three alpha-helices (alpha4-alpha6) is remarkably conserved, suggesting that it is the common structural motif for the CMD family proteins. In addition, the nine residues of the N-terminal tag bound to the cleft region between alpha1 and alpha3 in chains A and B of TTHA0727, implying that this region is the putative binding/active site for some small molecules.
About this Structure
2CWQ is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the conserved protein TTHA0727 from Thermus thermophilus HB8 at 1.9 A resolution: A CMD family member distinct from carboxymuconolactone decarboxylase (CMD) and AhpD., Ito K, Arai R, Fusatomi E, Kamo-Uchikubo T, Kawaguchi S, Akasaka R, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S, Protein Sci. 2006 May;15(5):1187-92. Epub 2006 Apr 5. PMID:16597838 Page seeded by OCA on Sat May 3 23:13:59 2008
Categories: Single protein | Thermus thermophilus | Arai, R. | Fusatomi, E. | Ito, K. | Kamo-Uchikubo, T. | Kawaguchi, S. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shirouzu, M. | Terada, T. | Yokoyama, S. | All alpha | Conserved hypothetical protein | National project on protein structural and functional analyse | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
