1WUB
Crystal structure of the polyisoprenoid-binding protein, TT1927b, from Thermus thermophilus HB8
「1UF6」から置き換えられました1WUB の概要
| エントリーDOI | 10.2210/pdb1wub/pdb |
| 分子名称 | 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) |
| 機能のキーワード | beta-barrel, structural genomics, riken structural genomics/proteomics initiative, rsgi, lipid binding protein |
| 由来する生物種 | Thermus thermophilus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 20220.91 |
| 構造登録者 | 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) (登録日: 2004-12-03, 公開日: 2004-12-21, 最終更新日: 2024-03-13) |
| 主引用文献 | 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 Cited by 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: 15741337DOI: 10.1110/ps.041183305 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.65 Å) |
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