2out | pdb_00002out

Solution Structure of HI1506, a Novel Two Domain Protein from Haemophilus influenzae

spinqualitylabelsall models 2out, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2out is a 1 chain structure with sequence from "bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: HI1506, HI1507 ("Bacterium influenzae" Lehmann and Neumann 1896) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed HI1506 is a 128-residue hypothetical protein of unknown function from Haemophilus influenzae. It was originally annotated as a shorter 85-residue protein, but a more detailed sequence analysis conducted in our laboratory revealed that the full-length protein has an additional 43 residues on the C terminus, corresponding with a region initially ascribed to HI1507. As part of a larger effort to understand the functions of hypothetical proteins from Gram-negative bacteria, and H. influenzae in particular, we report here the three-dimensional solution NMR structure for the corrected full-length HI1506 protein. The structure consists of two well-defined domains, an alpha/beta 50-residue N-domain and a 3-alpha 32-residue C-domain, separated by an unstructured 30-residue linker. Both domains have positively charged surface patches and weak structural homology with folds that are associated with RNA binding, suggesting a possible functional role in binding distal nucleic acid sites. Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae.,Sari N, He Y, Doseeva V, Surabian K, Ramprakash J, Schwarz F, Herzberg O, Orban J Protein Sci. 2007 May;16(5):977-82. Epub 2007 Mar 30. PMID:17400915 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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