2ov8: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ov8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_toyocaensis Streptomyces toyocaensis]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OV8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ov8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_toyocaensis Streptomyces toyocaensis]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OV8 FirstGlance]. <br> | ||
</td></tr><tr><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])</td></tr> | </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])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ov8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ov8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ov8 RCSB], [http://www.ebi.ac.uk/pdbsum/2ov8 PDBsum]</span></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=2ov8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ov8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ov8 RCSB], [http://www.ebi.ac.uk/pdbsum/2ov8 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Streptomyces toyocaensis]] | [[Category: Streptomyces toyocaensis]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Cygler, M | [[Category: Cygler, M]] | ||
[[Category: Matte, A | [[Category: Matte, A]] | ||
[[Category: Shi, R | [[Category: Shi, R]] | ||
[[Category: Bsgi]] | [[Category: Bsgi]] | ||
[[Category: Stal apoenzyme]] | [[Category: Stal apoenzyme]] | ||
[[Category: Sulfotransferase]] | [[Category: Sulfotransferase]] | ||
[[Category: Unknown function]] | [[Category: Unknown function]] | ||
Revision as of 06:37, 25 December 2014
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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