2out
From Proteopedia
(New page: 200px<br /><applet load="2out" size="350" color="white" frame="true" align="right" spinBox="true" caption="2out" /> '''Solution Structure of HI1506, a Novel Two Do...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | HI1506 is a 128-residue hypothetical protein of unknown function from | + | 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== | ==About this Structure== | ||
| Line 17: | Line 17: | ||
[[Category: Herzberg, O.]] | [[Category: Herzberg, O.]] | ||
[[Category: Orban, J.]] | [[Category: Orban, J.]] | ||
| - | [[Category: S2F, Structure | + | [[Category: S2F, Structure 2.Function Project.]] |
[[Category: Sari, N.]] | [[Category: Sari, N.]] | ||
[[Category: Schwarz, F.]] | [[Category: Schwarz, F.]] | ||
| Line 28: | Line 28: | ||
[[Category: structure 2 function project]] | [[Category: structure 2 function project]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:22:43 2008'' |
Revision as of 16:22, 21 February 2008
|
Solution Structure of HI1506, a Novel Two Domain Protein from Haemophilus influenzae
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
Page seeded by OCA on Thu Feb 21 18:22:43 2008
