2OUT
Solution Structure of HI1506, a Novel Two Domain Protein from Haemophilus influenzae
Summary for 2OUT
| Entry DOI | 10.2210/pdb2out/pdb |
| NMR Information | BMRB: 6780 |
| Descriptor | Mu-like prophage FluMu protein gp35, Protein HI1507 in Mu-like prophage FluMu region (1 entity in total) |
| Functional Keywords | structural genomics, haemophilus influenzae, hypothetical protein, structure 2 function project, s2f, unknown function |
| Biological source | Haemophilus influenzae |
| Total number of polymer chains | 1 |
| Total formula weight | 14139.68 |
| Authors | Sari, N.,He, Y.,Doseeva, V.,Surabian, K.,Schwarz, F.,Herzberg, O.,Orban, J.,Structure 2 Function Project (S2F) (deposition date: 2007-02-12, release date: 2007-05-01, Last modification date: 2024-05-22) |
| Primary citation | Sari, N.,He, Y.,Doseeva, V.,Surabian, K.,Ramprakash, J.,Schwarz, F.,Herzberg, O.,Orban, J. Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae. Protein Sci., 16:977-982, 2007 Cited by PubMed 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 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. PubMed: 17400915DOI: 10.1110/ps.072820907 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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