1WUB

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

Replaces:  1UF6

Summary for 1WUB

• Entry DOI: 10.2210/pdb1wub/pdb
• Descriptor: conserved hypothetical protein TT1927b, (2E,6E,10E,14E,18E,22E,26E)-3,7,11,15,19,23,27,31-OCTAMETHYLDOTRIACONTA-2,6,10,14,18,22,26,30-OCTAENYL TRIHYDROGEN DIPHOSPHATE (3 entities in total)
• Functional Keywords: beta-barrel, structural genomics, riken structural genomics/proteomics initiative, rsgi, lipid binding protein
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 20220.91

Authors

Handa, N.,Idaka, M.,Terada, T.,Hamana, H.,Ishizuka, Y.,Park, S.-Y.,Tame, J.R.H.,Doi-Katayama, Y.,Hirota, H.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-12-03, release date: 2004-12-21, Last modification date: 2024-03-13)

Primary citation

Handa, N.,Terada, T.,Doi-Katayama, Y.,Hirota, H.,Tame, J.R.,Park, S.-Y.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.
Crystal structure of a novel polyisoprenoid-binding protein from Thermus thermophilus HB8
Protein Sci., 14:1004-1010, 2005

PubMed 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.

PubMed: 15741337
DOI: 10.1110/ps.041183305

Experimental method

X-RAY DIFFRACTION (1.65 Å)