3mgb: Difference between revisions
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== | ==Teg 12 Ternary Structure Complexed with PAP and the Teicoplanin Aglycone== | ||
[[3mgb]] is a 4 chain structure with sequence from [ | <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 [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=3MGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MGB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04Å</td></tr> | |||
<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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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>, <scene name='pdbligand=PAP:3-PHOSPHATE-ADENOSINE-5-DIPHOSPHATE'>PAP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mgb OCA], [https://pdbe.org/3mgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mgb RCSB], [https://www.ebi.ac.uk/pdbsum/3mgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mgb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B7T1D7_9BACT B7T1D7_9BACT] | |||
== 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/main_output.php?pdb_ID=3mgb 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> | |||
<ref | |||
[[Category: Nonomuraea | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 3mgb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Nonomuraea gerenzanensis]] | |||
[[Category: Uncultured soil bacterium]] | [[Category: Uncultured soil bacterium]] | ||
[[Category: Banik | [[Category: Banik JJ]] | ||
[[Category: Bick | [[Category: Bick MJ]] | ||
[[Category: Brady | [[Category: Brady SF]] | ||
[[Category: Darst | [[Category: Darst SA]] | ||
Latest revision as of 08:53, 6 September 2023
Teg 12 Ternary Structure Complexed with PAP and the Teicoplanin Aglycone
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