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Solution structure of HI1506, a novel two‐domain protein from Haemophilus influenzae
Author(s) -
Sari Nese,
He Yanan,
Doseeva Victoria,
Surabian Karen,
Ramprakash Jayanthi,
Schwarz Fred,
Herzberg Osnat,
Orban John
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.072820907
Subject(s) - haemophilus influenzae , residue (chemistry) , linker , protein structure , peptide sequence , chemistry , nucleic acid , protein tertiary structure , crystallography , biophysics , biochemistry , stereochemistry , biology , antibiotics , computer science , gene , operating system
Abstract 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 α/β 50‐residue N‐domain and a 3‐α 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.