Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae.

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TitleSolution structure of HI1506, a novel two-domain protein from Haemophilus influenzae.
Publication TypeJournal Article
Year of Publication2007
AuthorsSari, N, He, Y, Doseeva, V, Surabian, K, Ramprakash, J, Schwarz, FP, Herzberg, O, Orban, J
JournalProtein Sci
Date Published2007 May
KeywordsAmino Acid Sequence, Bacterial Proteins, Calorimetry, Differential Scanning, Haemophilus influenzae, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Solutions

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.

Alternate JournalProtein Sci.
PubMed ID17400915
PubMed Central IDPMC2206629
Grant List1S10RR15744 / RR / NCRR NIH HHS / United States
GM57890 / GM / NIGMS NIH HHS / United States