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==Crystal Structure of I122A/I330A variant of S-adenosylmethionine synthetase from Cryptosporidium hominis in complex with ONB-SAM (2-nitro benzyme S-adenosyl-methionine)== | ==Crystal Structure of I122A/I330A variant of S-adenosylmethionine synthetase from Cryptosporidium hominis in complex with ONB-SAM (2-nitro benzyme S-adenosyl-methionine)== | ||
<StructureSection load='6ltv' size='340' side='right'caption='[[6ltv]]' scene=''> | <StructureSection load='6ltv' size='340' side='right'caption='[[6ltv]], [[Resolution|resolution]] 1.87Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LTV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LTV FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ltv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryho Cryho]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LTV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LTV FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ltv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ltv OCA], [http://pdbe.org/6ltv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ltv RCSB], [http://www.ebi.ac.uk/pdbsum/6ltv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ltv ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PO:TRIPHOSPHATE'>3PO</scene>, <scene name='pdbligand=EU9:[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-[(3R)-3-azanyl-4-oxidanyl-4-oxidanylidene-butyl]-[(2-nitrophenyl)methyl]sulfanium'>EU9</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHUDEA7_2650 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237895 CRYHO])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ltv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ltv OCA], [http://pdbe.org/6ltv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ltv RCSB], [http://www.ebi.ac.uk/pdbsum/6ltv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ltv ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/A0A0S4TKQ5_CRYHO A0A0S4TKQ5_CRYHO]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[RuleBase:RU000541] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Methylation and demethylation of DNA, RNA and proteins has emerged as a major regulatory mechanism. Studying the function of these modifications would benefit from tools for their site-specific inhibition and timed removal. S -Adenosyl-L-methionine (AdoMet) analogs in combination with methyltransferases (MTases) have proven useful to map or block and release MTase target sites, however their enzymatic generation has been limited to aliphatic groups at the sulfur atom. We engineered a SAM synthetase from Cryptosporidium hominis (PC-ChMAT) for efficient generation of AdoMet analogs with photocaging groups that are not accepted by any WT MAT reported to date. The crystal structure of PC-ChMAT at 1.87 A revealed how the photocaged AdoMet analog is accommodated and guided engineering of a thermostable MAT from Methanocaldococcus jannaschii . PC-MATs were compatible with DNA- and RNA MTases, enabling sequence-specific modification ("writing") of plasmid DNA and light-triggered removal ("erasing"). | |||
Engineered SAM synthetases for enzymatic generation of AdoMet analogs with photocaging groups and reversible DNA modification in cascade reactions.,Michailidou F, Klocker N, Cornelissen N, Singh RK, Peters A, Ovcharenko A, Kummel D, Rentmeister A Angew Chem Int Ed Engl. 2020 Oct 5. doi: 10.1002/anie.202012623. PMID:33017502<ref>PMID:33017502</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ltv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cryho]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kuemmel D]] | [[Category: Methionine adenosyltransferase]] | ||
[[Category: Michailidou F]] | [[Category: Kuemmel, D]] | ||
[[Category: Rentmeister A]] | [[Category: Michailidou, F]] | ||
[[Category: Singh | [[Category: Rentmeister, A]] | ||
[[Category: Singh, R K]] | |||
[[Category: S-adenosylmethionine synthetase]] | |||
[[Category: Transferase]] | |||
[[Category: Triphosphate]] | |||
Revision as of 11:59, 6 January 2021
Crystal Structure of I122A/I330A variant of S-adenosylmethionine synthetase from Cryptosporidium hominis in complex with ONB-SAM (2-nitro benzyme S-adenosyl-methionine)Crystal Structure of I122A/I330A variant of S-adenosylmethionine synthetase from Cryptosporidium hominis in complex with ONB-SAM (2-nitro benzyme S-adenosyl-methionine)
Structural highlights
Function[A0A0S4TKQ5_CRYHO] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[RuleBase:RU000541] Publication Abstract from PubMedMethylation and demethylation of DNA, RNA and proteins has emerged as a major regulatory mechanism. Studying the function of these modifications would benefit from tools for their site-specific inhibition and timed removal. S -Adenosyl-L-methionine (AdoMet) analogs in combination with methyltransferases (MTases) have proven useful to map or block and release MTase target sites, however their enzymatic generation has been limited to aliphatic groups at the sulfur atom. We engineered a SAM synthetase from Cryptosporidium hominis (PC-ChMAT) for efficient generation of AdoMet analogs with photocaging groups that are not accepted by any WT MAT reported to date. The crystal structure of PC-ChMAT at 1.87 A revealed how the photocaged AdoMet analog is accommodated and guided engineering of a thermostable MAT from Methanocaldococcus jannaschii . PC-MATs were compatible with DNA- and RNA MTases, enabling sequence-specific modification ("writing") of plasmid DNA and light-triggered removal ("erasing"). Engineered SAM synthetases for enzymatic generation of AdoMet analogs with photocaging groups and reversible DNA modification in cascade reactions.,Michailidou F, Klocker N, Cornelissen N, Singh RK, Peters A, Ovcharenko A, Kummel D, Rentmeister A Angew Chem Int Ed Engl. 2020 Oct 5. doi: 10.1002/anie.202012623. PMID:33017502[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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