1lva: Difference between revisions

Revision as of 22:24, 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:1lva.png

Template:STRUCTURE 1lva

Crystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor SelBCrystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor SelB

Template:ABSTRACT PUBMED 12145214

About this StructureAbout this Structure

1LVA is a Single protein structure of sequence from Moorella thermoacetica. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB., Selmer M, Su XD, EMBO J. 2002 Aug 1;21(15):4145-53. PMID:12145214

Page seeded by OCA on Wed Jul 2 22:24:35 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1lva.gif|left|200px]]
+{{Seed}}
+[[Image:1lva.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1lva|  PDB=1lva  |  SCENE=  }}
-'''Crystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor SelB'''
+===Crystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor SelB===
-==Overview==
+<!--
-SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). We present the crystal structure of a C-terminal fragment of SelB (SelB-C) from Moorella thermoacetica at 2.12 A resolution, solved by a combination of selenium and yttrium multiwavelength anomalous dispersion. This 264 amino acid fragment contains the entire C-terminal extension beginning after the EF-Tu-homologous domains. SelB-C consists of four similar winged-helix domains arranged into the shape of an L. This is the first example of winged-helix domains involved in RNA binding. The location of conserved basic amino acids, together with data from the literature, define the position of the mRNA-binding site. Steric requirements indicate that a conformational change may occur upon ribosome interaction. Structural observations and data in the literature suggest that this change happens upon mRNA binding.
+The line below this paragraph, {{ABSTRACT_PUBMED_12145214}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12145214 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12145214}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Su, X D.]]
 [[Category: Winged-helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:19:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 22:24:35 2008''