Premium
Crystal structure of a novel polyisoprenoid‐binding protein from Thermus thermophilus HB8
Author(s) -
Handa Noriko,
Terada Takaho,
DoiKatayama Yukiko,
Hirota Hiroshi,
Tame Jeremy R.H.,
Park SamYong,
Kuramitsu Seiki,
Shirouzu Mikako,
Yokoyama Shigeyuki
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.041183305
Subject(s) - thermus thermophilus , antiparallel (mathematics) , structural genomics , lipocalin , biochemistry , protein structure , chemistry , protein family , biology , crystallography , stereochemistry , gene , physics , escherichia coli , quantum mechanics , magnetic field
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 β‐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.