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'''Structure-based functional identification of a novel heme-binding protein from thermus thermophilus HB8''' | '''Structure-based functional identification of a novel heme-binding protein from thermus thermophilus HB8''' | ||
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==About this Structure== | ==About this Structure== | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VDH OCA]. | |||
==Reference== | ==Reference== | ||
Structure-based functional identification of a novel heme-binding protein from Thermus thermophilus HB8., Ebihara A, Okamoto A, Kousumi Y, Yamamoto H, Masui R, Ueyama N, Yokoyama S, Kuramitsu S, J Struct Funct Genomics. 2005;6(1):21-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15965735 15965735] | Structure-based functional identification of a novel heme-binding protein from Thermus thermophilus HB8., Ebihara A, Okamoto A, Kousumi Y, Yamamoto H, Masui R, Ueyama N, Yokoyama S, Kuramitsu S, J Struct Funct Genomics. 2005;6(1):21-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15965735 15965735] | ||
[[Category: Ebihara, A.]] | [[Category: Ebihara, A.]] | ||
[[Category: Inoue, Y.]] | [[Category: Inoue, Y.]] | ||
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[[Category: Yamamoto, H.]] | [[Category: Yamamoto, H.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: | [[Category: Beta barrel]] | ||
[[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 12:24:31 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 09:24, 3 May 2008
Structure-based functional identification of a novel heme-binding protein from thermus thermophilus HB8
Overview
The TT1485 gene from Thermus thermophilus HB8 encodes a hypothetical protein of unknown function with about 20 sequence homologs of bacterial or archaeal origin. Together they form a family of uncharacterized proteins, the cluster of orthologous group COG3253. Using a combination of amino acid sequence analysis, three-dimensional structural studies and biochemical assays, we identified TT1485 as a novel heme-binding protein. The crystal structure reveals that this protein is a pentamer and each monomer exhibits a beta-barrel fold. TT1485 is structurally similar to muconolactone isomerase, but this provided no functional clues. Amino acid sequence analysis revealed remote homology to a heme enzyme, chlorite dismutase. Strikingly, amino acid residues that are highly conserved in the homologous hypothetical proteins and chlorite dismutase cluster around a deep cavity on the surface of each monomer. Molecular modeling shows that the cavity can accommodate a heme group with a strictly conserved His as a heme ligand. TT1485 reconstituted with iron protoporphyrin IX chloride gave a low chlorite dismutase activity, indicating that TT1485 catalyzes a reaction other than chlorite degradation. The presence of a possible Fe-His-Asp triad in the heme proximal site suggests that TT1485 functions as a novel heme peroxidase to detoxify hydrogen peroxide within the cell.
About this Structure
Full crystallographic information is available from OCA.
Reference
Structure-based functional identification of a novel heme-binding protein from Thermus thermophilus HB8., Ebihara A, Okamoto A, Kousumi Y, Yamamoto H, Masui R, Ueyama N, Yokoyama S, Kuramitsu S, J Struct Funct Genomics. 2005;6(1):21-32. PMID:15965735 Page seeded by OCA on Sat May 3 12:24:31 2008
