2k3f: Difference between revisions

Revision as of 22:50, 27 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:2k3f.png

Template:STRUCTURE 2k3f

Ribosomal protein L11 from Thermotoga maritimaRibosomal protein L11 from Thermotoga maritima

Template:ABSTRACT PUBMED 16094695

About this StructureAbout this Structure

2K3F is a Single protein structure of sequence from Thermotoga maritima. Full experimental information is available from OCA.

ReferenceReference

Domain reorientation and induced fit upon RNA binding: solution structure and dynamics of ribosomal protein L11 from Thermotoga maritima., Ilin S, Hoskins A, Ohlenschlager O, Jonker HR, Schwalbe H, Wohnert J, Chembiochem. 2005 Sep;6(9):1611-8. PMID:16094695

L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy., Jonker HR, Ilin S, Grimm SK, Wohnert J, Schwalbe H, Nucleic Acids Res. 2007;35(2):441-54. Epub 2006 Dec 14. PMID:17169991

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 {{STRUCTURE_2k3f|  PDB=2k3f  |  SCENE=  }}
-'''Ribosomal protein L11 from Thermotoga maritima'''
+===Ribosomal protein L11 from Thermotoga maritima===
-==Overview==
+<!--
-L11, a protein of the large ribosomal subunit, binds to a highly conserved domain of 23S rRNA and mediates ribosomal GTPase activity. Its C-terminal domain is the main determinant for rRNA binding, whereas its N-terminal domain plays only a limited role in RNA binding. The N-terminal domain is thought to be involved in interactions with elongation and release factors as well as with the antibiotics thiostrepton and micrococcin. This report presents the NMR solution structure of the full-length L11 protein from the thermophilic eubacterium Thermotoga maritima in its free form. The structure is based on a large number of orientational restraints derived from residual dipolar couplings in addition to conventional NOE-based restraints. The solution structure of L11 demonstrates that, in contrast to many other multidomain RNA-binding proteins, the relative orientation of the two domains is well defined. This is shown both by heteronuclear 15N-relaxation and residual dipolar-coupling data. Comparison of this NMR structure with the X-ray structure of RNA-bound L11, reveals that binding not only induces a rigidification of a flexible loop in the C-terminal domain, but also a sizeable reorientation of the N-terminal domain. The domain orientation in free L11 shows limited similarity to that of ribosome-bound L11 in complex with elongation factor, EF-G.
+The line below this paragraph, {{ABSTRACT_PUBMED_16094695}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16094695 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16094695}}
 ==About this Structure==
-K3F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K3F OCA].
+K3F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K3F OCA].
 ==Reference==
 Domain reorientation and induced fit upon RNA binding: solution structure and dynamics of ribosomal protein L11 from Thermotoga maritima., Ilin S, Hoskins A, Ohlenschlager O, Jonker HR, Schwalbe H, Wohnert J, Chembiochem. 2005 Sep;6(9):1611-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16094695 16094695]
+L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy., Jonker HR, Ilin S, Grimm SK, Wohnert J, Schwalbe H, Nucleic Acids Res. 2007;35(2):441-54. Epub 2006 Dec 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17169991 17169991]
 [[Category: Single protein]]
 [[Category: Thermotoga maritima]]
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 [[Category: Ribosomal protein]]
 [[Category: Rna-binding]]
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