1X9A

Solution NMR Structure of Protein Tm0979 from Thermotoga maritima. Ontario Center for Structural Proteomics Target TM0979_1_87; Northeast Structural Genomics Consortium Target VT98.

1X9A の概要

• エントリーDOI: 10.2210/pdb1x9a/pdb
• NMR情報: BMRB: 6324
• 分子名称: hypothetical protein TM0979 (1 entity in total)
• 機能のキーワード: structural genomics, protein structure initiative, psi, northeast structural genomics consortium, nesg, ocsp, hypothetical protein, beta-alpha protein, dimer, unknown function
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24119.41

構造登録者

Gaspar, J.A.,Liu, C.,Vassall, K.A.,Stathopulos, P.B.,Meglei, G.,Stephen, R.,Pineda-Lucena, A.,Wu, B.,Yee, A.,Arrowsmith, C.H.,Meiering, E.M.,Northeast Structural Genomics Consortium (NESG) (登録日: 2004-08-20, 公開日: 2004-12-07, 最終更新日: 2024-05-22)

主引用文献

Gaspar, J.A.,Liu, C.,Vassall, K.A.,Meglei, G.,Stephen, R.,Stathopulos, P.B.,Pineda-Lucena, A.,Wu, B.,Yee, A.,Arrowsmith, C.H.,Meiering, E.M.
A novel member of the YchN-like fold: solution structure of the hypothetical protein Tm0979 from Thermotoga maritima.
Protein Sci., 14:216-223, 2005

PubMed Abstract: We report herein the NMR structure of Tm0979, a structural proteomics target from Thermotoga maritima. The Tm0979 fold consists of four beta/alpha units, which form a central parallel beta-sheet with strand order 1234. The first three helices pack toward one face of the sheet and the fourth helix packs against the other face. The protein forms a dimer by adjacent parallel packing of the fourth helices sandwiched between the two beta-sheets. This fold is very interesting from several points of view. First, it represents the first structure determination for the DsrH family of conserved hypothetical proteins, which are involved in oxidation of intracellular sulfur but have no defined molecular function. Based on structure and sequence analysis, possible functions are discussed. Second, the fold of Tm0979 most closely resembles YchN-like folds; however the proteins that adopt these folds differ in secondary structural elements and quaternary structure. Comparison of these proteins provides insight into possible mechanisms of evolution of quaternary structure through a simple mechanism of hydrophobicity-changing mutations of one or two residues. Third, the Tm0979 fold is found to be similar to flavodoxin-like folds and beta/alpha barrel proteins, and may provide a link between these very abundant folds and putative ancestral half-barrel proteins.

PubMed: 15608123
DOI: 10.1110/ps.041068605

実験手法

SOLUTION NMR