3mg9

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{{STRUCTURE_3mg9| PDB=3mg9 | SCENE= }}
 
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===Teg 12 Binary Structure Complexed with the Teicoplanin Aglycone===
 
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{{ABSTRACT_PUBMED_20361791}}
 
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==About this Structure==
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==Teg 12 Binary Structure Complexed with the Teicoplanin Aglycone==
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[[3mg9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Nonomuraea_sp._atcc_39727 Nonomuraea sp. atcc 39727] and [http://en.wikipedia.org/wiki/Uncultured_soil_bacterium Uncultured soil bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MG9 OCA].
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<StructureSection load='3mg9' size='340' side='right'caption='[[3mg9]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3mg9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Nonomuraea_gerenzanensis Nonomuraea gerenzanensis] and [https://en.wikipedia.org/wiki/Uncultured_soil_bacterium Uncultured soil bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MG9 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3FG:(2S)-AMINO(3,5-DIHYDROXYPHENYL)ETHANOIC+ACID'>3FG</scene>, <scene name='pdbligand=3MY:3-CHLORO-D-TYROSINE'>3MY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GHP:(2R)-AMINO(4-HYDROXYPHENYL)ETHANOIC+ACID'>GHP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OMY:(BETAR)-3-CHLORO-BETA-HYDROXY-L-TYROSINE'>OMY</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mg9 OCA], [https://pdbe.org/3mg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mg9 RCSB], [https://www.ebi.ac.uk/pdbsum/3mg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mg9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B7T1D7_9BACT B7T1D7_9BACT]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mg/3mg9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3mg9 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The TEG gene cluster, a glycopeptide biosynthetic gene cluster that is predicted to encode the biosynthesis of a polysulfated glycopeptide congener, was recently cloned from DNA extracted directly from desert soil. This predicted glycopeptide gene cluster contains three closely related sulfotransferases (Teg12, -13, and -14) that sulfate teicoplanin-like glycopeptides at three unique sites. Here we report a series of structures: an apo structure of Teg12, Teg12 bound to the desulfated cosubstrate 3'-phosphoadenosine 5'-phosphate, and Teg12 bound to the teicoplanin aglycone. Teg12 appears to undergo a series of significant conformational rearrangements during glycopeptide recruitment, binding, and catalysis. Loop regions that exhibit the most conformational flexibility show the least sequence conservation between TEG sulfotransferases. Site-directed mutagenesis guided by our structural studies confirmed the importance of key catalytic residues as well as the importance of residues found throughout the conformationally flexible loop regions.
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==Reference==
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Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone.,Bick MJ, Banik JJ, Darst SA, Brady SF Biochemistry. 2010 May 18;49(19):4159-68. PMID:20361791<ref>PMID:20361791</ref>
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<ref group="xtra">PMID:020361791</ref><references group="xtra"/><references/>
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[[Category: Nonomuraea sp. atcc 39727]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3mg9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Nonomuraea gerenzanensis]]
[[Category: Uncultured soil bacterium]]
[[Category: Uncultured soil bacterium]]
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[[Category: Banik, J J.]]
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[[Category: Banik JJ]]
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[[Category: Bick, M J.]]
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[[Category: Bick MJ]]
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[[Category: Brady, S F.]]
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[[Category: Brady SF]]
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[[Category: Darst, S A.]]
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[[Category: Darst SA]]
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[[Category: Antibiotic]]
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[[Category: Glyopeptide]]
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[[Category: Sulfotransferase]]
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[[Category: Transferase-antibiotic complex]]
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Current revision

Teg 12 Binary Structure Complexed with the Teicoplanin Aglycone

PDB ID 3mg9

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