1jw2 | pdb_00001jw2

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

spinqualitylabelsall models 1jw2 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1jw2 is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function HHA_ECOLI Down-regulates hemolysin production and can also stimulate transposition events in vivo. Binds DNA and influences DNA topology in response to environmental stimuli. Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR. Decreases biofilm formation by repressing the transcription of fimbrial genes fimA and ihfA, and by repressing the transcription of tRNAs corresponding to rare codons, which are abundant in type 1 fimbrial genes. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. An NMR approach to structural proteomics.,Yee A, Chang X, Pineda-Lucena A, Wu B, Semesi A, Le B, Ramelot T, Lee GM, Bhattacharyya S, Gutierrez P, Denisov A, Lee CH, Cort JR, Kozlov G, Liao J, Finak G, Chen L, Wishart D, Lee W, McIntosh LP, Gehring K, Kennedy MA, Edwards AM, Arrowsmith CH Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1825-30. PMID:11854485 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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