1lva: Difference between revisions
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|PDB= 1lva |SIZE=350|CAPTION= <scene name='initialview01'>1lva</scene>, resolution 2.12Å | |PDB= 1lva |SIZE=350|CAPTION= <scene name='initialview01'>1lva</scene>, resolution 2.12Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=Y1:YTTRIUM+ION'>Y1</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SelB(amino acids 370-634) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1525 Moorella thermoacetica]) | |GENE= SelB(amino acids 370-634) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1525 Moorella thermoacetica]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lva OCA], [http://www.ebi.ac.uk/pdbsum/1lva PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lva RCSB]</span> | |||
}} | }} | ||
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[[Category: Selmer, M.]] | [[Category: Selmer, M.]] | ||
[[Category: Su, X D.]] | [[Category: Su, X D.]] | ||
[[Category: winged-helix]] | [[Category: winged-helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:07:47 2008'' | ||
Revision as of 19:07, 30 March 2008
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| 1lva, resolution 2.12Å | |||||||||||||
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| Ligands: | MSE, SO4, Y1 | ||||||||||||
| Gene: | SelB(amino acids 370-634) (Moorella thermoacetica) | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.
About this Structure
1LVA is a Single protein structure of sequence from Moorella thermoacetica. Full crystallographic information is available from OCA.
Reference
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
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