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New page: '''Unreleased structure''' The entry 3lst is ON HOLD Authors: Chang, A., Singh, S., Bingman, C.A., Thorson, J.S., Phillips Jr., G.N., Center for Eukaryotic Structural Genomics (CESG) D... |
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The | ==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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3LST FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lst OCA], [https://pdbe.org/3lst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lst RCSB], [https://www.ebi.ac.uk/pdbsum/3lst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lst ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8KNE5_MICEC Q8KNE5_MICEC] | |||
== 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/initialview03.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/main_output.php?pdb_ID=3lst 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> | |||
<div class="pdbe-citations 3lst" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Micromonospora echinospora]] | |||
[[Category: Bingman CA]] | |||
[[Category: Chang A]] | |||
[[Category: Phillips Jr GN]] | |||
[[Category: Singh S]] | |||
[[Category: Thorson JS]] | |||
Latest revision as of 08:58, 17 October 2024
Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound formCrystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form
Structural highlights
FunctionEvolutionary 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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