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1T72

Crystal structure of phosphate transport system protein phoU from Aquifex aeolicus

1T72 の概要
エントリーDOI10.2210/pdb1t72/pdb
分子名称Phosphate transport system protein phoU homolog (2 entities in total)
機能のキーワードhelix bundle, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, transport protein
由来する生物種Aquifex aeolicus
細胞内の位置Cytoplasm (By similarity): O67053
タンパク質・核酸の鎖数6
化学式量合計158482.27
構造登録者
Oganesyan, V.,Kim, S.-H.,Oganesyan, N.,Jancarik, J.,Adams, P.D.,Kim, R.,Berkeley Structural Genomics Center (BSGC) (登録日: 2004-05-07, 公開日: 2004-12-07, 最終更新日: 2024-11-13)
主引用文献Oganesyan, V.,Oganesyan, N.,Adams, P.D.,Jancarik, J.,Yokota, H.A.,Kim, R.,Kim, S.H.
Crystal structure of the "PhoU-like" phosphate uptake regulator from Aquifex aeolicus.
J.Bacteriol., 187:4238-4244, 2005
Cited by
PubMed Abstract: The phoU gene of Aquifex aeolicus encodes a protein called PHOU_AQUAE with sequence similarity to the PhoU protein of Escherichia coli. Despite the fact that there is a large number of family members (more than 300) attributed to almost all known bacteria and despite PHOU_AQUAE's association with the regulation of genes for phosphate metabolism, the nature of its regulatory function is not well understood. Nearly one-half of these PhoU-like proteins, including both PHOU_AQUAE and the one from E. coli, form a subfamily with an apparent dimer structure of two PhoU domains on the basis of their amino acid sequence. The crystal structure of PHOU_AQUAE (a 221-amino-acid protein) reveals two similar coiled-coil PhoU domains, each forming a three-helix bundle. The structures of PHOU_AQUAE proteins from both a soluble fraction and refolded inclusion bodies (at resolutions of 2.8 and 3.2A, respectively) showed no significant differences. The folds of the PhoU domain and Bag domains (for a class of cofactors of the eukaryotic chaperone Hsp70 family) are similar. Accordingly, we propose that gene regulation by PhoU may occur by association of PHOU_AQUAE with the ATPase domain of the histidine kinase PhoR, promoting release of its substrate PhoB. Other proteins that share the PhoU domain fold include the coiled-coil domains of the STAT protein, the ribosome-recycling factor, and structural proteins like spectrin.
PubMed: 15937186
DOI: 10.1128/JB.187.12.4238-4244.2005
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.9 Å)
構造検証レポート
Validation report summary of 1t72
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-04-09に公開中

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