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==Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form==
==Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form==
<StructureSection load='3lst' size='340' side='right' caption='[[3lst]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3lst' size='340' side='right' caption='[[3lst]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<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='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 ATCC 15837])</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 ATCC 15837])</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://pdbe.org/3lst PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lst RCSB], [http://www.ebi.ac.uk/pdbsum/3lst 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=3lst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lst OCA], [http://pdbe.org/3lst PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lst RCSB], [http://www.ebi.ac.uk/pdbsum/3lst PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lst ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==

Revision as of 12:02, 1 November 2017

Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound formCrystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form

Structural highlights

3lst is a 2 chain structure with sequence from Atcc 15837. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
NonStd Res:
Gene:calO1 (ATCC 15837)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Chang A, Singh S, Bingman CA, Thorson JS, Phillips GN Jr. Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway. Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):197-203. Epub 2011, Feb 15. PMID:21358050 doi:10.1107/S090744491100360X

3lst, resolution 2.40Å

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