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1JW2

SOLUTION STRUCTURE OF HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha FROM ESCHERICHIA COLI. Ontario Centre for Structural Proteomics target EC0308_1_72; Northeast Structural Genomics Target ET88

Summary for 1JW2
Entry DOI10.2210/pdb1jw2/pdb
NMR InformationBMRB: 5166
DescriptorHEMOLYSIN EXPRESSION MODULATING PROTEIN Hha (1 entity in total)
Functional Keywordshha, hemolysin expression modulating protein, structural genomics, protein structure initiative, ocsp, nesg, psi, northeast structural genomics consortium, gene regulation
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight8642.02
Authors
Chang, X.,Yee, A.,Savchenko, A.,Edwards, A.M.,Arrowsmith, C.H.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2001-09-02, release date: 2002-02-27, Last modification date: 2024-05-22)
Primary citationYee, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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