2out | pdb_00002out
Solution Structure of HI1506, a Novel Two Domain Protein from Haemophilus influenzae
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Overview
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.
About this Structure
2OUT is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
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
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