1m8v: Difference between revisions

Revision as of 23:27, 2 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:1m8v.png

Template:STRUCTURE 1m8v

Structure of Pyrococcus abyssii Sm Protein in Complex with a Uridine HeptamerStructure of Pyrococcus abyssii Sm Protein in Complex with a Uridine Heptamer

Template:ABSTRACT PUBMED 12409299

About this StructureAbout this Structure

1M8V is a Single protein structure of sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA. Common features of RNA binding in archaea and eukarya., Thore S, Mayer C, Sauter C, Weeks S, Suck D, J Biol Chem. 2003 Jan 10;278(2):1239-47. Epub 2002 Oct 29. PMID:12409299

Page seeded by OCA on Wed Jul 2 23:27:34 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1m8v.gif|left|200px]]
+{{Seed}}
+[[Image:1m8v.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1m8v|  PDB=1m8v  |  SCENE=  }}
-'''Structure of Pyrococcus abyssii Sm Protein in Complex with a Uridine Heptamer'''
+===Structure of Pyrococcus abyssii Sm Protein in Complex with a Uridine Heptamer===
-==Overview==
+<!--
-The Sm proteins are conserved in all three domains of life and are always associated with U-rich RNA sequences. Their proposed function is to mediate RNA-RNA interactions. We present here the crystal structures of Pyrococcus abyssi Sm protein (PA-Sm1) and its complex with a uridine heptamer. The overall structure of the protein complex, a heptameric ring with a central cavity, is similar to that proposed for the eukaryotic Sm core complex and found for other archaeal Sm proteins. RNA molecules bind to the protein at two different sites. They interact specifically inside the ring with three highly conserved residues, defining the uridine-binding pocket. In addition, nucleotides also interact on the surface formed by the N-terminal alpha-helix as well as a conserved aromatic residue in beta-strand 2 of the PA-Sm1 protein. The mutation of this conserved aromatic residue shows the importance of this second site for the discrimination between RNA sequences. Given the high structural homology between archaeal and eukaryotic Sm proteins, the PA-Sm1.RNA complex provides a model for how the small nuclear RNA contacts the Sm proteins in the Sm core. In addition, it suggests how Sm proteins might exert their function as modulators of RNA-RNA interactions.
+The line below this paragraph, {{ABSTRACT_PUBMED_12409299}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12409299 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12409299}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Protein-rna complex]]
 [[Category: Sm protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:46:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 23:27:34 2008''