1wub

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spinqualitylabelsall models 1wub, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the polyisoprenoid-binding protein, TT1927b, from Thermus thermophilus HB8

Overview

The isoprenoid quinones exist widely among prokaryotes and eukaryotes., They play essential roles in respiratory electron transport and in, controlling oxidative stress and gene regulation. In the isoprenoid, quinone biosynthetic pathway, polyprenyl pyrophosphates are used as, isoprenoid side-chain precursors. Here we report the crystal structure of, a novel polyprenyl pyrophosphate binding protein, TT1927b, from Thermus, thermophilus HB8, complexed with its ligand. This protein belongs to the, YceI-like family in the Pfam database, and its sequence homologs are, present in a broad range of bacteria and archaea. The structure consists, of an extended, eight-stranded, antiparallel beta-barrel. In the, hydrophobic pore of the barrel, the protein binds the polyisoprenoid chain, by hydrophobic interactions. Its overall structure resembles the lipocalin, fold, but there is no sequence homology between TT1927b and the lipocalin, family of proteins.

About this Structure

1WUB is a Single protein structure of sequence from Thermus thermophilus with OTP as ligand. This structure superseeds the now removed PDB entry 1UF6. Full crystallographic information is available from OCA.

Reference

Crystal structure of a novel polyisoprenoid-binding protein from Thermus thermophilus HB8., Handa N, Terada T, Doi-Katayama Y, Hirota H, Tame JR, Park SY, Kuramitsu S, Shirouzu M, Yokoyama S, Protein Sci. 2005 Apr;14(4):1004-10. Epub 2005 Mar 1. PMID:15741337

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