3mgb: Difference between revisions
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==Teg 12 Ternary Structure Complexed with PAP and the Teicoplanin Aglycone== | |||
<StructureSection load='3mgb' size='340' side='right' caption='[[3mgb]], [[Resolution|resolution]] 2.04Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3mgb]] is a 4 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=3MGB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MGB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PAP:3-PHOSPHATE-ADENOSINE-5-DIPHOSPHATE'>PAP</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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=GHP:(2R)-AMINO(4-HYDROXYPHENYL)ETHANOIC+ACID'>GHP</scene>, <scene name='pdbligand=OMY:(BETAR)-3-CHLORO-BETA-HYDROXY-L-TYROSINE'>OMY</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mg9|3mg9]], [[2wdx|2wdx]], [[3mgc|3mgc]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TEG1, TEG12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=164851 uncultured soil bacterium])</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=3mgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mgb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mgb RCSB], [http://www.ebi.ac.uk/pdbsum/3mgb PDBsum]</span></td></tr> | |||
</table> | |||
== 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/mg/3mgb_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Nonomuraea sp. atcc 39727]] | [[Category: Nonomuraea sp. atcc 39727]] | ||
[[Category: Uncultured soil bacterium]] | [[Category: Uncultured soil bacterium]] | ||
[[Category: Banik, J J | [[Category: Banik, J J]] | ||
[[Category: Bick, M J | [[Category: Bick, M J]] | ||
[[Category: Brady, S F | [[Category: Brady, S F]] | ||
[[Category: Darst, S A | [[Category: Darst, S A]] | ||
[[Category: Antibiotic]] | [[Category: Antibiotic]] | ||
[[Category: Glycopeptide]] | [[Category: Glycopeptide]] | ||
[[Category: Sulfotransferase]] | [[Category: Sulfotransferase]] | ||
[[Category: Transferase-antibiotic complex]] | [[Category: Transferase-antibiotic complex]] | ||