Crystal Structure of a Novel Polyisoprenoid-binding Protein from Thermus Thermophilus HB8

Overview

Journal Protein Sci

Specialty Biochemistry

Date 2005 Mar 3

PMID 15741337

Citations 18

Authors

Noriko Handa

Takaho Terada

Yukiko Doi-Katayama

Hiroshi Hirota

Jeremy R H Tame

Sam-Yong Park

Seiki Kuramitsu

Mikako Shirouzu

Shigeyuki Yokoyama

Affiliations

Soon will be listed here.

Abstract

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.

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