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2ov8

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[[Image:2ov8.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of StaL==
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|PDB= 2ov8 |SIZE=350|CAPTION= <scene name='initialview01'>2ov8</scene>, resolution 2.580&Aring;
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<StructureSection load='2ov8' size='340' side='right'caption='[[2ov8]], [[Resolution|resolution]] 2.58&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</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>
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|GENE= stal ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=55952 Streptomyces toyocaensis])
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<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>
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}}
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</table>
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== Evolutionary Conservation ==
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'''Crystal Structure of StaL'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ov/2ov8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2ov8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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).
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).
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==About this Structure==
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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<ref>PMID:17329243</ref>
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2OV8 is a [[Single protein]] structure of 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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17329243 17329243]
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[[Category: Single protein]]
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[[Category: Streptomyces toyocaensis]]
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
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[[Category: Cygler, M.]]
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[[Category: Matte, A.]]
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[[Category: Shi, R.]]
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[[Category: bsgi]]
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[[Category: montreal-kingston bacterial structural genomics initiative]]
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[[Category: stal apoenzyme]]
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[[Category: structural genomic]]
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[[Category: sulfotransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:04:54 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ov8" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Streptomyces toyocaensis nishimura et al]]
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[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Cygler, M]]
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[[Category: Matte, A]]
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[[Category: Shi, R]]
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[[Category: Bsgi]]
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[[Category: Stal apoenzyme]]
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[[Category: Sulfotransferase]]
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[[Category: Unknown function]]

Current revision

Crystal Structure of StaL

PDB ID 2ov8

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