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| | ==Teg 12 Binary Structure Complexed with the Teicoplanin Aglycone== | | ==Teg 12 Binary Structure Complexed with the Teicoplanin Aglycone== |
| - | <StructureSection load='3mg9' size='340' side='right' caption='[[3mg9]], [[Resolution|resolution]] 2.27Å' scene=''> | + | <StructureSection load='3mg9' size='340' side='right'caption='[[3mg9]], [[Resolution|resolution]] 2.27Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[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/Soil_bacterium_48-1 Soil bacterium 48-1]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MG9 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27Å</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>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mgb|3mgb]], [[2wdx|2wdx]], [[3mgc|3mgc]]</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=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> |
| - | <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 soil bacterium 48-1])</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=3mg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mg9 OCA], [http://pdbe.org/3mg9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mg9 RCSB], [http://www.ebi.ac.uk/pdbsum/3mg9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mg9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B7T1D7_9BACT B7T1D7_9BACT] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Nonomuraea sp. atcc 39727]] | + | [[Category: Large Structures]] |
| - | [[Category: Soil bacterium 48-1]] | + | [[Category: Nonomuraea gerenzanensis]] |
| - | [[Category: Banik, J J]] | + | [[Category: Uncultured soil bacterium]] |
| - | [[Category: Bick, M J]] | + | [[Category: Banik JJ]] |
| - | [[Category: Brady, S F]] | + | [[Category: Bick MJ]] |
| - | [[Category: Darst, S A]] | + | [[Category: Brady SF]] |
| - | [[Category: Antibiotic]] | + | [[Category: Darst SA]] |
| - | [[Category: Glyopeptide]]
| + | |
| - | [[Category: Sulfotransferase]]
| + | |
| - | [[Category: Transferase-antibiotic complex]]
| + | |
| Structural highlights
3mg9 is a 3 chain structure with sequence from Nonomuraea gerenzanensis and Uncultured soil bacterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.27Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
B7T1D7_9BACT
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bick MJ, Banik JJ, Darst SA, Brady SF. Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone. Biochemistry. 2010 May 18;49(19):4159-68. PMID:20361791 doi:10.1021/bi100150v
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