1x7o
From Proteopedia
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|PDB= 1x7o |SIZE=350|CAPTION= <scene name='initialview01'>1x7o</scene>, resolution 2.37Å | |PDB= 1x7o |SIZE=350|CAPTION= <scene name='initialview01'>1x7o</scene>, resolution 2.37Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1x7p|1X7P]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x7o OCA], [http://www.ebi.ac.uk/pdbsum/1x7o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1x7o RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: spou]] | [[Category: spou]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:45:51 2008'' |
Revision as of 21:45, 30 March 2008
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| , resolution 2.37Å | |||||||
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| Ligands: | |||||||
| Related: | 1X7P
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the SpoU Methyltransferase AviRb from Streptomyces viridochromogenes
Overview
The emergence of antibiotic-resistant bacterial strains is a widespread problem in medical practice and drug design, and each case requires the elucidation of the underlying mechanism. AviRb from Streptomyces viridochromogenes methylates the 2'-O atom of U2479 of the 23S ribosomal RNA in Gram-positive bacteria and thus mediates resistance to the oligosaccharide (orthosomycin) antibiotic avilamycin. The structure of AviRb with and without bound cofactor S-adenosyl-L-methionine (AdoMet) was determined, showing that it is a homodimer belonging to the SpoU family within the SPOUT class of methyltransferases. The relationships within this class were analyzed in detail and, in addition, a novel fourth SpoU sequence fingerprint is proposed. Each subunit of AviRb consists of two domains. The N-terminal domain, being related to the ribosomal proteins L30 and L7Ae, is likely to bind RNA. The C-terminal domain is related to all SPOUT methyltransferases, and is responsible for AdoMet-binding, catalysis and dimerization. The cofactor binds at the characteristic knot of the polypeptide in an unusually bent conformation. The transferred methyl group points to a broad cleft formed with the L30-type domain of the other subunit. Measurements of mutant activity revealed four important residues responsible for catalysis and allowed the modeling of a complex between AviRb and the RNA target. The model includes a specificity pocket for uracil but does not contain a base for deprotonating the 2'-O atom of U2479 on methylation.
About this Structure
1X7O is a Single protein structure of sequence from Streptomyces viridochromogenes. Full crystallographic information is available from OCA.
Reference
Structure and function of the antibiotic resistance-mediating methyltransferase AviRb from Streptomyces viridochromogenes., Mosbacher TG, Bechthold A, Schulz GE, J Mol Biol. 2005 Jan 21;345(3):535-45. PMID:15581897
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