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==Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form== | |||
<StructureSection load='3lst' size='340' side='right' caption='[[3lst]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3lst]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Micromonospora_echinospora Micromonospora echinospora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LST FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">calO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1877 Micromonospora echinospora])</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=3lst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lst OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lst RCSB], [http://www.ebi.ac.uk/pdbsum/3lst PDBsum]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ls/3lst_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The X-ray structure determination at 2.4 A resolution of the putative orsellinic acid C3 O-methyltransferase (CalO1) involved in calicheamicin biosynthesis is reported. Comparison of CalO1 with a homology model of the functionally related calicheamicin orsellinic acid C2 O-methyltransferase (CalO6) implicates several residues that are likely to contribute to the regiospecificity of alkylation. Consistent with the proposed requirement of an acyl-carrier-protein-bound substrate, this structural study also reveals structural determinants within CalO1 that are anticipated to accommodate an association with an acyl carrier protein. | |||
Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway.,Chang A, Singh S, Bingman CA, Thorson JS, Phillips GN Jr Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):197-203. Epub 2011, Feb 15. PMID:21358050<ref>PMID:21358050</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Micromonospora echinospora]] | [[Category: Micromonospora echinospora]] | ||
[[Category: Bingman, C A | [[Category: Bingman, C A]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Chang, A | [[Category: Chang, A]] | ||
[[Category: Phillips, G N | [[Category: Phillips, G N]] | ||
[[Category: Singh, S | [[Category: Singh, S]] | ||
[[Category: Thorson, J S | [[Category: Thorson, J S]] | ||
[[Category: Calicheamicin]] | [[Category: Calicheamicin]] | ||
[[Category: Calo1]] | [[Category: Calo1]] | ||
[[Category: Cesg]] | [[Category: Cesg]] | ||
[[Category: Enediyne]] | [[Category: Enediyne]] | ||
[[Category: Methyltransferase]] | [[Category: Methyltransferase]] | ||
[[Category: Protein structure initiative | [[Category: PSI, Protein structure initiative]] | ||
[[Category: Sah]] | [[Category: Sah]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 18:01, 18 December 2014
Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound formCrystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form
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 PubMedThe X-ray structure determination at 2.4 A resolution of the putative orsellinic acid C3 O-methyltransferase (CalO1) involved in calicheamicin biosynthesis is reported. Comparison of CalO1 with a homology model of the functionally related calicheamicin orsellinic acid C2 O-methyltransferase (CalO6) implicates several residues that are likely to contribute to the regiospecificity of alkylation. Consistent with the proposed requirement of an acyl-carrier-protein-bound substrate, this structural study also reveals structural determinants within CalO1 that are anticipated to accommodate an association with an acyl carrier protein. Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway.,Chang A, Singh S, Bingman CA, Thorson JS, Phillips GN Jr Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):197-203. Epub 2011, Feb 15. PMID:21358050[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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