1pyb: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= metG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus]) | |GENE= metG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1pxf|1PXF]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pyb OCA], [http://www.ebi.ac.uk/pdbsum/1pyb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pyb RCSB]</span> | |||
}} | }} | ||
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[[Category: oligosaccharide-binding fold]] | [[Category: oligosaccharide-binding fold]] | ||
''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 23:06:11 2008'' | ||
Revision as of 23:06, 30 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | metG (Aquifex aeolicus) | ||||||
| Related: | 1PXF
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Aquifex aeolicus Trbp111: a Stucture-Specific tRNA Binding Protein
OverviewOverview
Trbp111 is a 111 amino acid Aquifex aeolicus structure-specific tRNA-binding protein that has homologous counterparts distributed throughout evolution. A dimer is the functional unit for binding a single tRNA. Here we report the 3D structures of the A.aeolicus protein and its Escherichia coli homolog at resolutions of 2.50 and 1.87 A, respectively. The structure shows a symmetrical dimer of two core domains and a central dimerization domain where the N- and C-terminal regions of Trbp111 form an extensive dimer interface. The core of the monomer is a classical oligonucleotide/oligosaccharide-binding (OB) fold with a five-stranded ss-barrel and a small capping helix. This structure is similar to that seen in the anticodon-binding domain of three class II tRNA synthetases and several other proteins. Mutational analysis identified sites important for interactions with tRNA. These residues line the inner surfaces of two clefts formed between the ss-barrel of each monomer and the dimer interface. The results are consistent with a proposed model for asymmetrical docking of the convex side of tRNA to the dimer.
About this StructureAbout this Structure
1PYB is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of trbp111: a structure-specific tRNA-binding protein., Swairjo MA, Morales AJ, Wang CC, Ortiz AR, Schimmel P, EMBO J. 2000 Dec 1;19(23):6287-98. PMID:11101501
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