1o9g: Difference between revisions

Revision as of 00:53, 12 September 2015

RRNA METHYLTRANSFERASE AVIRA FROM STREPTOMYCES VIRIDOCHROMOGENES AT 1.5A

Structural highlights

1o9g is a 1 chain structure with sequence from "actinomyces_viridochromogenes"_krainsky_1914 "actinomyces viridochromogenes" krainsky 1914. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	MSE
Related:	1qam, 1qan, 1qao, 1qaq, 1yub
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[AVRA_STRVR] Specifically methylates the guanine-2535 in 23S ribosomal RNA. Confers resistance to antibiotic avilamycin, an orthosomycin antibiotic.^[1] ^[2]

Publication Abstract from PubMed

The emergence of antibiotic-resistant bacterial strains is a widespread problem in contemporary medical practice and drug design. It is therefore important to elucidate the underlying mechanism in each case. The methyltransferase AviRa from Streptomyces viridochromogenes mediates resistance to the antibiotic avilamycin, which is closely related to evernimicin, an oligosaccharide antibiotic that has been used in medical studies. The structure of AviRa was determined by X-ray diffraction at 1.5A resolution. Phases were obtained from one selenomethionine residue introduced by site-directed mutagenesis. The chain-fold is similar to that of most methyltransferases, although AviRa contains two additional helices as a specific feature. A putative-binding site for the cofactor S-adenosyl-L-methionine was derived from homologous structures. It agrees with the conserved pattern of interacting amino acid residues. AviRa methylates a specific guanine base within the peptidyltransferase loop of the 23S ribosomal RNA. Guided by the target, the enzyme was docked to the cognate ribosomal surface, where it fit well into a deep cleft without contacting any ribosomal protein. The two additional alpha-helices of AviRa filled a depression in the surface. Since the transferred methyl group of the cofactor is in a pocket beneath the enzyme surface, the targeted guanine base has to flip out for methylation.

Crystal structure of the avilamycin resistance-conferring methyltransferase AviRa from Streptomyces viridochromogenes.,Mosbacher TG, Bechthold A, Schulz GE J Mol Biol. 2003 May 23;329(1):147-57. PMID:12742024^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Weitnauer G, Gaisser S, Trefzer A, Stockert S, Westrich L, Quiros LM, Mendez C, Salas JA, Bechthold A. An ATP-binding cassette transporter and two rRNA methyltransferases are involved in resistance to avilamycin in the producer organism Streptomyces viridochromogenes Tu57. Antimicrob Agents Chemother. 2001 Mar;45(3):690-5. PMID:11181344 doi:https://dx.doi.org/10.1128/AAC.45.3.690-695.2001
↑ Treede I, Jakobsen L, Kirpekar F, Vester B, Weitnauer G, Bechthold A, Douthwaite S. The avilamycin resistance determinants AviRa and AviRb methylate 23S rRNA at the guanosine 2535 base and the uridine 2479 ribose. Mol Microbiol. 2003 Jul;49(2):309-18. PMID:12828631
↑ Mosbacher TG, Bechthold A, Schulz GE. Crystal structure of the avilamycin resistance-conferring methyltransferase AviRa from Streptomyces viridochromogenes. J Mol Biol. 2003 May 23;329(1):147-57. PMID:12742024

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OCA

[1] Weitnauer G, Gaisser S, Trefzer A, Stockert S, Westrich L, Quiros LM, Mendez C, Salas JA, Bechthold A. An ATP-binding cassette transporter and two rRNA methyltransferases are involved in resistance to avilamycin in the producer organism Streptomyces viridochromogenes Tu57. Antimicrob Agents Chemother. 2001 Mar;45(3):690-5. PMID:11181344 doi:https://dx.doi.org/10.1128/AAC.45.3.690-695.2001

[2] Treede I, Jakobsen L, Kirpekar F, Vester B, Weitnauer G, Bechthold A, Douthwaite S. The avilamycin resistance determinants AviRa and AviRb methylate 23S rRNA at the guanosine 2535 base and the uridine 2479 ribose. Mol Microbiol. 2003 Jul;49(2):309-18. PMID:12828631

[3] Mosbacher TG, Bechthold A, Schulz GE. Crystal structure of the avilamycin resistance-conferring methyltransferase AviRa from Streptomyces viridochromogenes. J Mol Biol. 2003 May 23;329(1):147-57. PMID:12742024

[1]

[2]

[3]

@@ Line 2: / Line 2: @@
 <StructureSection load='1o9g' size='340' side='right' caption='[[1o9g]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1o9g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_viridochromogenes Streptomyces viridochromogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O9G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1o9g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_viridochromogenes"_krainsky_1914 "actinomyces viridochromogenes" krainsky 1914]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O9G FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qam|1qam]], [[1qan|1qan]], [[1qao|1qao]], [[1qaq|1qaq]], [[1yub|1yub]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o9g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o9g RCSB], [http://www.ebi.ac.uk/pdbsum/1o9g PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o9g OCA], [http://pdbe.org/1o9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o9g RCSB], [http://www.ebi.ac.uk/pdbsum/1o9g PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/AVRA_STRVR AVRA_STRVR]] Specifically methylates the guanine-2535 in 23S ribosomal RNA. Confers resistance to antibiotic avilamycin, an orthosomycin antibiotic.<ref>PMID:11181344</ref> <ref>PMID:12828631</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 15: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1o9g" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Streptomyces viridochromogenes]]
+[[Category: Actinomyces viridochromogenes krainsky 1914]]
 [[Category: Mosbacher, T G]]
 [[Category: Schulz, G E]]

1o9g: Difference between revisions

Revision as of 00:53, 12 September 2015

RRNA METHYLTRANSFERASE AVIRA FROM STREPTOMYCES VIRIDOCHROMOGENES AT 1.5A

Structural highlights

Function

Publication Abstract from PubMed

References

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