1EIJ

NMR ENSEMBLE OF METHANOBACTERIUM THERMOAUTOTROPHICUM PROTEIN 1615

1EIJ の概要

• エントリーDOI: 10.2210/pdb1eij/pdb
• 分子名称: HYPOTHETICAL PROTEIN MTH1615 (1 entity in total)
• 機能のキーワード: beta-helix, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, dna binding protein
• 由来する生物種: Methanothermobacter thermautotrophicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9576.51

構造登録者

Christendat, D.,Booth, V.,Gernstein, M.,Arrowsmith, C.H.,Edwards, A.M.,Northeast Structural Genomics Consortium (NESG) (登録日: 2000-02-25, 公開日: 2000-11-03, 最終更新日: 2024-05-22)

主引用文献

Christendat, D.,Yee, A.,Dharamsi, A.,Kluger, Y.,Savchenko, A.,Cort, J.R.,Booth, V.,Mackereth, C.D.,Saridakis, V.,Ekiel, I.,Kozlov, G.,Maxwell, K.L.,Wu, N.,McIntosh, L.P.,Gehring, K.,Kennedy, M.A.,Davidson, A.R.,Pai, E.F.,Gerstein, M.,Edwards, A.M.,Arrowsmith, C.H.
Structural proteomics of an archaeon.
Nat.Struct.Biol., 7:903-909, 2000

PubMed Abstract: A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, approximately 20% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility, implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics.

PubMed: 11017201
DOI: 10.1038/82823

実験手法

SOLUTION NMR