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Structure of a UPF0150-family protein from Thermus thermophilus HB8.

ABSTRACT: TTHA0281 is a hypothetical protein from Thermus thermophilus HB8 that belongs to an uncharacterized protein family, UPF0150, in the Pfam database and to COG1598 in the National Center for Biotechnology Information Database of Clusters of Orthologous Groups. The X-ray crystal structure of the protein was determined by a multiple-wavelength anomalous dispersion technique and was refined at 1.9 A resolution to a final R factor of 18.5%. The TTHA0281 monomer adopts an alpha-beta-beta-beta-alpha fold and forms a homotetramer. Based on the properties and functions of structural homologues of the TTHA0281 monomer, the TTHA0281 protein is speculated to be involved in RNA metabolism, including RNA binding and cleavage.

SUBMITTER: Okazaki N

PROVIDER: S-EPMC2330186 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature

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Structure of a UPF0150-family protein from Thermus thermophilus HB8.

Okazaki Nobuo N Kumei Maki M Manzoku Miho M Kuramitsu Seiki S Shirouzu Mikako M Shinkai Akeo A Yokoyama Shigeyuki S

Acta crystallographica. Section F, Structural biology and crystallization communications 20070223 Pt 3

TTHA0281 is a hypothetical protein from Thermus thermophilus HB8 that belongs to an uncharacterized protein family, UPF0150, in the Pfam database and to COG1598 in the National Center for Biotechnology Information Database of Clusters of Orthologous Groups. The X-ray crystal structure of the protein was determined by a multiple-wavelength anomalous dispersion technique and was refined at 1.9 A resolution to a final R factor of 18.5%. The TTHA0281 monomer adopts an alpha-beta-beta-beta-alpha fold ...[more]

PMID: 17329807

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Transcriptional repression mediated by a TetR family protein, PfmR, from Thermus thermophilus HB8.

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Structure of the minimized alpha/beta-hydrolase fold protein from Thermus thermophilus HB8.

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Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8.

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Crystal structure of enoyl-CoA hydratase from Thermus thermophilus HB8.

Project description:Fatty-acid degradation is an oxidative process that involves four enzymatic steps and is referred to as the β-oxidation pathway. During this process, long-chain acyl-CoAs are broken down into acetyl-CoA, which enters the mitochondrial tricarboxylic acid (TCA) cycle, resulting in the production of energy in the form of ATP. Enoyl-CoA hydratase (ECH) catalyzes the second step of the β-oxidation pathway by the syn addition of water to the double bond between C2 and C3 of a 2-trans-enoyl-CoA, resulting in the formation of a 3-hydroxyacyl CoA. Here, the crystal structure of ECH from Thermus thermophilus HB8 (TtECH) is reported at 2.85 Å resolution. TtECH forms a hexamer as a dimer of trimers, and wide clefts are uniquely formed between the two trimers. Although the overall structure of TtECH is similar to that of a hexameric ECH from Rattus norvegicus (RnECH), there is a significant shift in the positions of the helices and loops around the active-site region, which includes the replacement of a longer α3 helix with a shorter α-helix and 310-helix in RnECH. Additionally, one of the catalytic residues of RnECH, Glu144 (numbering based on the RnECH enzyme), is replaced by a glycine in TtECH, while the other catalytic residue Glu164, as well as Ala98 and Gly141 that stabilize the enolate intermediate, is conserved. Their putative ligand-binding sites and active-site residue compositions are dissimilar.

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Crystal structure of elongation factor P from Thermus thermophilus HB8.

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Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8.

Project description:TTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape.

| S-EPMC2675583 | biostudies-literature

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