2pjp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pjp.gif|left|200px]]<br /><applet load="2pjp" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2pjp.gif|left|200px]]
-
caption="2pjp, resolution 2.300&Aring;" />
+
 
-
'''Structure of the mRNA-binding domain of elongation factor SelB from E.coli in complex with SECIS RNA'''<br />
+
{{Structure
 +
|PDB= 2pjp |SIZE=350|CAPTION= <scene name='initialview01'>2pjp</scene>, resolution 2.300&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
 +
|ACTIVITY=
 +
|GENE= selB, fdhA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
 +
}}
 +
 
 +
'''Structure of the mRNA-binding domain of elongation factor SelB from E.coli in complex with SECIS RNA'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2PJP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PJP OCA].
+
2PJP is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PJP OCA].
==Reference==
==Reference==
-
Structural insight into a molecular switch in tandem winged-helix motifs from elongation factor SelB., Soler N, Fourmy D, Yoshizawa S, J Mol Biol. 2007 Jul 20;370(4):728-41. Epub 2007 May 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17537456 17537456]
+
Structural insight into a molecular switch in tandem winged-helix motifs from elongation factor SelB., Soler N, Fourmy D, Yoshizawa S, J Mol Biol. 2007 Jul 20;370(4):728-41. Epub 2007 May 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17537456 17537456]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 28: Line 37:
[[Category: winged-helix]]
[[Category: winged-helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:11 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:13:50 2008''

Revision as of 16:13, 20 March 2008

Image:2pjp.gif


PDB ID 2pjp

Drag the structure with the mouse to rotate
, resolution 2.300Å
Ligands: , , and
Gene: selB, fdhA (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



Structure of the mRNA-binding domain of elongation factor SelB from E.coli in complex with SECIS RNA


Overview

Elongation factor SelB is responsible for co-translational incorporation of selenocysteine (Sec) into proteins. The UGA stop codon is recoded as a Sec codon in the presence of a downstream mRNA hairpin. In prokaryotes, in addition to the EF-Tu-like N-terminal domains, a C-terminal extension containing four tandem winged-helix motifs (WH1-4) recognizes the mRNA hairpin. The 2.3-A resolution crystal structure of the Escherichia coli WH3/4 domains bound to mRNA with mutagenesis data reveal that the two WH motifs use the same structural elements to bind RNA. The structure together with the 2.6-A resolution structure of the WH1-4 domains from Moorella thermoacetica bound to RNA revealed that a salt bridge connecting WH2 to WH3 modules is disrupted upon mRNA binding. The results provide a structural basis for the molecular switch that may allow communication between tRNA and mRNA binding sites and illustrate how RNA acts as an activator of the switch. The structures show that tandem WH motifs not only provide an excellent scaffold for RNA binding but can also have an active role in the function of protein-RNA complexes.

About this Structure

2PJP is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural insight into a molecular switch in tandem winged-helix motifs from elongation factor SelB., Soler N, Fourmy D, Yoshizawa S, J Mol Biol. 2007 Jul 20;370(4):728-41. Epub 2007 May 10. PMID:17537456

Page seeded by OCA on Thu Mar 20 18:13:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pjp"
Personal tools