1hk9: Difference between revisions

Revision as of 08:18, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1hk9.png

Template:STRUCTURE 1hk9

CRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLICRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 12853626

About this StructureAbout this Structure

1HK9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli., Sauter C, Basquin J, Suck D, Nucleic Acids Res. 2003 Jul 15;31(14):4091-8. PMID:12853626

Page seeded by OCA on Tue Jul 1 08:18:21 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1hk9.jpg|left|200px]]
+{{Seed}}
+[[Image:1hk9.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1hk9|  PDB=1hk9  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLI'''
+===CRYSTAL STRUCTURE OF THE HFQ PROTEIN FROM ESCHERICHIA COLI===
-==Overview==
+<!--
-The Hfq protein was discovered in Escherichia coli in the early seventies as a host factor for the Qbeta phage RNA replication. During the last decade, it was shown to be involved in many RNA processing events and remote sequence homology indicated a link to spliceosomal Sm proteins. We report the crystal structure of the E.coli Hfq protein showing that its monomer displays a characteristic Sm-fold and forms a homo-hexamer, in agreement with former biochemical data. Overall, the structure of the E.coli Hfq ring is similar to the one recently described for Staphylococcus aureus. This confirms that bacteria contain a hexameric Sm-like protein which is likely to be an ancient and less specialized form characterized by a relaxed RNA binding specificity. In addition, we identified an Hfq ortholog in the archaeon Methanococcus jannaschii which lacks a classical Sm/Lsm gene. Finally, a detailed structural comparison shows that the Sm-fold is remarkably well conserved in bacteria, Archaea and Eukarya, and represents a universal and modular building unit for oligomeric RNA binding proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_12853626}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12853626 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12853626}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Rna chaperone]]
 [[Category: Sm-like]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:56:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:18:21 2008''