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| | ==Crystal Structure of StaL-sulfate complex== | | ==Crystal Structure of StaL-sulfate complex== |
| - | <StructureSection load='2ovb' size='340' side='right' caption='[[2ovb]], [[Resolution|resolution]] 2.61Å' scene=''> | + | <StructureSection load='2ovb' size='340' side='right'caption='[[2ovb]], [[Resolution|resolution]] 2.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ovb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_toyocaensis"_nishimura_et_al. "streptomyces toyocaensis" nishimura et al.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OVB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ovb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_toyocaensis Streptomyces toyocaensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OVB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.61Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">stal ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=55952 "Streptomyces toyocaensis" Nishimura et al.])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2ovb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ovb OCA], [http://pdbe.org/2ovb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ovb RCSB], [http://www.ebi.ac.uk/pdbsum/2ovb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ovb ProSAT]</span></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=2ovb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ovb OCA], [https://pdbe.org/2ovb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ovb RCSB], [https://www.ebi.ac.uk/pdbsum/2ovb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ovb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/STAL_STRTO STAL_STRTO] Catalyzes the sulfonation of desulfo-A47934, the final step of A47934 biosynthesis. Has also weak activity in vitro with teicoplanin aglycone and teicoplanin.<ref>PMID:16492565</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ov/2ovb_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ov/2ovb_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptomyces toyocaensis nishimura et al]] | + | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]] | + | [[Category: Streptomyces toyocaensis]] |
| - | [[Category: Cygler, M]] | + | [[Category: Cygler M]] |
| - | [[Category: Matte, A]] | + | [[Category: Matte A]] |
| - | [[Category: Shi, R]] | + | [[Category: Shi R]] |
| - | [[Category: Bsgi]]
| + | |
| - | [[Category: Stal sulfate complex]]
| + | |
| - | [[Category: Sulfotransferase]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
STAL_STRTO Catalyzes the sulfonation of desulfo-A47934, the final step of A47934 biosynthesis. Has also weak activity in vitro with teicoplanin aglycone and teicoplanin.[1]
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
Over the past decade, antimicrobial resistance has emerged as a major public health crisis. Glycopeptide antibiotics such as vancomycin and teicoplanin are clinically important for the treatment of Gram-positive bacterial infections. StaL is a 3'-phosphoadenosine 5'-phosphosulfate-dependent sulfotransferase capable of sulfating the cross-linked heptapeptide substrate both in vivo and in vitro, yielding the product A47934, a unique teicoplanin-class glycopeptide antibiotic. The sulfonation reaction catalyzed by StaL constitutes the final step in A47934 biosynthesis. Here we report the crystal structure of StaL and its complex with the cofactor product 3'-phosphoadenosine 5'-phosphate. This is only the second prokaryotic sulfotransferase to be structurally characterized. StaL belongs to the large sulfotransferase family and shows higher similarity to cytosolic sulfotransferases (ST) than to the bacterial ST (Stf0). StaL has a novel dimerization motif, different from any other STs that have been structurally characterized. We have also applied molecular modeling to investigate the binding mode of the unique substrate, desulfo-A47934. Based on the structural analysis and modeling results, a series of residues was mutated and kinetically characterized. In addition to the conserved residues (Lys(12), His(67), and Ser(98)), molecular modeling, fluorescence quenching experiments, and mutagenesis studies identified several other residues essential for substrate binding and/or activity, including Trp(34), His(43), Phe(77), Trp(132), and Glu(205).
Crystal structure of StaL, a glycopeptide antibiotic sulfotransferase from Streptomyces toyocaensis.,Shi R, Lamb SS, Bhat S, Sulea T, Wright GD, Matte A, Cygler M J Biol Chem. 2007 Apr 27;282(17):13073-86. Epub 2007 Feb 28. PMID:17329243[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lamb SS, Patel T, Koteva KP, Wright GD. Biosynthesis of sulfated glycopeptide antibiotics by using the sulfotransferase StaL. Chem Biol. 2006 Feb;13(2):171-81. doi: 10.1016/j.chembiol.2005.12.003. PMID:16492565 doi:http://dx.doi.org/10.1016/j.chembiol.2005.12.003
- ↑ Shi R, Lamb SS, Bhat S, Sulea T, Wright GD, Matte A, Cygler M. Crystal structure of StaL, a glycopeptide antibiotic sulfotransferase from Streptomyces toyocaensis. J Biol Chem. 2007 Apr 27;282(17):13073-86. Epub 2007 Feb 28. PMID:17329243 doi:10.1074/jbc.M611912200
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