1JCU

Solution Structure of MTH1692 Protein from Methanobacterium thermoautotrophicum

1JCU の概要

• エントリーDOI: 10.2210/pdb1jcu/pdb
• NMR情報: BMRB: 5051
• 分子名称: conserved protein MTH1692 (1 entity in total)
• 機能のキーワード: mixed alpha-beta structure, structural genomics
• 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: 22642.18

構造登録者

Kozlov, G.,Ekiel, I.,Gehring, K. (登録日: 2001-06-11, 公開日: 2002-07-24, 最終更新日: 2024-05-22)

主引用文献

Yee, A.,Chang, X.,Pineda-Lucena, A.,Wu, B.,Semesi, A.,Le, B.,Ramelot, T.,Lee, G.M.,Bhattacharyya, S.,Gutierrez, P.,Denisov, A.,Lee, C.H.,Cort, J.R.,Kozlov, G.,Liao, J.,Finak, G.,Chen, L.,Wishart, D.,Lee, W.,McIntosh, L.P.,Gehring, K.,Kennedy, M.A.,Edwards, A.M.,Arrowsmith, C.H.
An NMR approach to structural proteomics.
Proc.Natl.Acad.Sci.USA, 99:1825-1830, 2002

PubMed Abstract: The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMR. Although there was variability among proteomes, overall 20% of these proteins were found to be readily amenable to NMR structure determination. NMR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins.

PubMed: 11854485
DOI: 10.1073/pnas.042684599

実験手法

SOLUTION NMR