2qtx
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2qtx.jpg|left|200px]] | [[Image:2qtx.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2qtx", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | | | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | + | --> | |
| - | + | {{STRUCTURE_2qtx| PDB=2qtx | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal structure of an Hfq-like protein from Methanococcus jannaschii''' | '''Crystal structure of an Hfq-like protein from Methanococcus jannaschii''' | ||
| Line 32: | Line 29: | ||
[[Category: Nielsen, J S.]] | [[Category: Nielsen, J S.]] | ||
[[Category: Valentin-Hansen, P.]] | [[Category: Valentin-Hansen, P.]] | ||
| - | [[Category: | + | [[Category: Hfq]] |
| - | [[Category: | + | [[Category: Rna binding protein]] |
| - | [[Category: | + | [[Category: Rna-binding protein]] |
| - | [[Category: | + | [[Category: Sm]] |
| - | [[Category: | + | [[Category: Srna]] |
| - | [[Category: | + | [[Category: Translational regulation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:40:36 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:40, 4 May 2008
Crystal structure of an Hfq-like protein from Methanococcus jannaschii
Overview
The Sm and Sm-like proteins are conserved in all three domains of life and have emerged as important players in many different RNA-processing reactions. Their proposed role is to mediate RNA-RNA and/or RNA-protein interactions. In marked contrast to eukaryotes, bacteria appear to contain only one distinct Sm-like protein belonging to the Hfq family of proteins. Similarly, there are generally only one or two subtypes of Sm-related proteins in archaea, but at least one archaeon, Methanococcus jannaschii, encodes a protein that is related to Hfq. This archaeon does not contain any gene encoding a conventional archaeal Sm-type protein, suggesting that Hfq proteins and archaeal Sm-homologs can complement each other functionally. Here, we report the functional characterization of M. jannaschii Hfq and its crystal structure at 2.5 A resolution. The protein forms a hexameric ring. The monomer fold, as well as the overall structure of the complex is similar to that found for the bacterial Hfq proteins. However, clear differences are seen in the charge distribution on the distal face of the ring, which is unusually negative in M. jannaschii Hfq. Moreover, owing to a very short N-terminal alpha-helix, the overall diameter of the archaeal Hfq hexamer is significantly smaller than its bacterial counterparts. Functional analysis reveals that Escherichia coli and M. jannaschii Hfqs display very similar biochemical and biological properties. It thus appears that the archaeal and bacterial Hfq proteins are largely functionally interchangeable.
About this Structure
2QTX is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
An Hfq-like protein in archaea: crystal structure and functional characterization of the Sm protein from Methanococcus jannaschii., Nielsen JS, Boggild A, Andersen CB, Nielsen G, Boysen A, Brodersen DE, Valentin-Hansen P, RNA. 2007 Dec;13(12):2213-23. Epub 2007 Oct 24. PMID:17959927 Page seeded by OCA on Sun May 4 15:40:36 2008
