1x7p: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
New page: left|200px<br /><applet load="1x7p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x7p, resolution 2.55Å" /> '''Crystal structure of...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1x7p.gif|left|200px]]<br /><applet load="1x7p" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1x7p, resolution 2.55&Aring;" />
'''Crystal structure of the SpoU Methyltransferase AviRb from Streptomyces viridochromogenes in complex with the cofactor AdoMet'''<br />


==Overview==
==Crystal structure of the SpoU Methyltransferase AviRb from Streptomyces viridochromogenes in complex with the cofactor AdoMet==
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.
<StructureSection load='1x7p' size='340' side='right'caption='[[1x7p]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1x7p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_viridochromogenes Streptomyces viridochromogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X7P FirstGlance]. <br>
1X7P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_viridochromogenes Streptomyces viridochromogenes] with SAM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X7P OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1x7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x7p OCA], [https://pdbe.org/1x7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x7p RCSB], [https://www.ebi.ac.uk/pdbsum/1x7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x7p ProSAT]</span></td></tr>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15581897 15581897]
</table>
[[Category: Single protein]]
== Function ==
[https://www.uniprot.org/uniprot/AVRB_STRVR AVRB_STRVR] Specifically methylates the 2'-O-ribose position of uridine-2479 in 23S ribosomal RNA. Confers resistance to antibiotic avilamycin, an orthosomycin antibiotic.<ref>PMID:11181344</ref> <ref>PMID:12828631</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x7/1x7p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1x7p ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces viridochromogenes]]
[[Category: Streptomyces viridochromogenes]]
[[Category: Bechthold, A.]]
[[Category: Bechthold A]]
[[Category: Mosbacher, T.G.]]
[[Category: Mosbacher TG]]
[[Category: Schulz, G.E.]]
[[Category: Schulz GE]]
[[Category: SAM]]
[[Category: bound cofactor adomet]]
[[Category: c-terminal knot]]
[[Category: spou]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:35:03 2007''
Retrieved from "https://proteopedia.org/1x7p"