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[[Image:1mr7.gif|left|200px]]


{{Structure
==Crystal Structure of Streptogramin A Acetyltransferase==
|PDB= 1mr7 |SIZE=350|CAPTION= <scene name='initialview01'>1mr7</scene>, resolution 1.80&Aring;
<StructureSection load='1mr7' size='340' side='right'caption='[[1mr7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1mr7]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MR7 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr7 OCA], [https://pdbe.org/1mr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mr7 RCSB], [https://www.ebi.ac.uk/pdbsum/1mr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mr7 ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[1mr9|1MR9]], [[1mrl|1MRL]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mr7 OCA], [http://www.ebi.ac.uk/pdbsum/1mr7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mr7 RCSB]</span>
[https://www.uniprot.org/uniprot/VATD_ENTFC VATD_ENTFC] Inactivates the A compounds of streptogramin antibiotics by acetylation, thus providing resistance to these antibiotics.
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''Crystal Structure of Streptogramin A Acetyltransferase'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mr/1mr7_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
Synercid, a new semisynthetic streptogramin-derived antibiotic containing dalfopristin and quinupristin, is used in treatment of life-threatening infections caused by glycopeptide-resistant Enterococcus faecium and other bacterial pathogens. However, dissemination of genes encoding virginiamycin acetyltransferases, enzymes that confer resistance to streptogramins, threatens to limit the medical utility of the quinupristin-dalfopristin combination. Here we present structures of virginiamycin acetyltransferase D (VatD) determined at 1.8 A resolution in the absence of ligands, at 2.8 A resolution bound to dalfopristin, and at 3.0 A resolution in the presence of acetyl-coenzyme A. Dalfopristin is bound by VatD in a similar conformation to that described previously for the streptogramin virginiamycin M1. However, specific interactions with the substrate are altered as a consequence of a conformational change in the pyrollidine ring that is propagated to adjacent constituents of the dalfopristin macrocycle. Inactivation of dalfopristin involves acetyl transfer from acetyl-coenzyme A to the sole (O-18) hydroxy group of the antibiotic that lies close to the side chain of the strictly conserved residue, His-82. Replacement of residue 82 by alanine is accompanied by a fall in specific activity of &gt;105-fold, indicating that the imidazole moiety of His-82 is a major determinant of catalytic rate enhancement by VatD. The structure of the VatD-dalfopristin complex can be used to predict positions where further structural modification of the drug might preclude enzyme binding and thereby circumvent Synercid resistance.
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==About this Structure==
</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=1mr7 ConSurf].
1MR7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR7 OCA].  
<div style="clear:both"></div>
 
__TOC__
==Reference==
</StructureSection>
Structural basis of Synercid (quinupristin-dalfopristin) resistance in Gram-positive bacterial pathogens., Kehoe LE, Snidwongse J, Courvalin P, Rafferty JB, Murray IA, J Biol Chem. 2003 Aug 8;278(32):29963-70. Epub 2003 May 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12771141 12771141]
[[Category: Enterococcus faecium]]
[[Category: Enterococcus faecium]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Courvalin, P.]]
[[Category: Courvalin P]]
[[Category: Kehoe, L E.]]
[[Category: Kehoe LE]]
[[Category: Murray, I A.]]
[[Category: Murray IA]]
[[Category: Rafferty, J B.]]
[[Category: Rafferty JB]]
[[Category: Snidwongse, J.]]
[[Category: Snidwongse J]]
[[Category: left-handed parallel beta-helix domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:20:02 2008''

Latest revision as of 13:27, 13 March 2024

Crystal Structure of Streptogramin A Acetyltransferase

1mr7, resolution 1.80Å

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