| Literature DB >> 16511226 |
Makoto Nakabayashi1, Naoki Shibata, Hirofumi Komori, Yasufumi Ueda, Hitoshi Iino, Akio Ebihara, Seiki Kuramitsu, Yoshiki Higuchi.
Abstract
The crystal structure of a conserved hypothetical protein, TTHA0849 from Thermus thermophilus HB8, has been determined at 2.4 A resolution as a part of a structural and functional genomics project on T. thermophilus HB8. The main-chain folding shows a compact alpha+beta motif, forming a hydrophobic cavity in the molecule. A structural similarity search reveals that it resembles those steroidogenic acute regulatory proteins that contain the lipid-transfer (START) domain, even though TTHA0849 shows comparatively weak sequence identity to polyketide cyclases. However, the size of the ligand-binding cavity is distinctly smaller than other START domain-containing proteins, suggesting that it catalyses the transfer of smaller ligand molecules.Entities:
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Year: 2005 PMID: 16511226 PMCID: PMC1978151 DOI: 10.1107/S1744309105035372
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091