2ov8: Difference between revisions
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==Crystal Structure of StaL== | ==Crystal Structure of StaL== | ||
<StructureSection load='2ov8' size='340' side='right' caption='[[2ov8]], [[Resolution|resolution]] 2.58Å' scene=''> | <StructureSection load='2ov8' size='340' side='right'caption='[[2ov8]], [[Resolution|resolution]] 2.58Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ov8]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2ov8]] is a 1 chain structure with sequence from [https://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=2OV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OV8 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">stal ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">stal ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=55952 "Streptomyces toyocaensis" Nishimura et al.])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ov8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ov8 OCA], [https://pdbe.org/2ov8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ov8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ov8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ov8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ov/2ov8_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ov/2ov8_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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</StructureSection> | </StructureSection> | ||
[[Category: Streptomyces toyocaensis nishimura et al]] | [[Category: Streptomyces toyocaensis nishimura et al]] | ||
[[Category: Large Structures]] | |||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Cygler, M]] | [[Category: Cygler, M]] | ||
Revision as of 16:06, 9 June 2021
Crystal Structure of StaLCrystal Structure of StaL
Structural highlights
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 PubMedOver 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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