1RYJ

Solution NMR Structure of Protein Mth1743 from Methanobacterium thermoautotrophicum. Ontario Centre for Structural Proteomics target MTH1743_1_70; Northeast Structural Genomics Consortium Target TT526.

Replaces:  1JSB

Summary for 1RYJ

• Entry DOI: 10.2210/pdb1ryj/pdb
• NMR Information: BMRB: 5106
• Descriptor: unknown (1 entity in total)
• Functional Keywords: beta/alpha protein, structural genomics, protein structure initiative, ocsp, nesg, psi, northeast structural genomics consortium, unknown function
• Biological source: Methanothermococcus thermolithotrophicus
• Total number of polymer chains: 1
• Total formula weight: 7765.07

Authors

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.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2003-12-22, release date: 2004-02-24, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

SOLUTION NMR