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Structural characterization of the mitomycin 7‐ O ‐methyltransferase

dc.contributor.authorSingh, Shanterien_US
dc.contributor.authorChang, Aramen_US
dc.contributor.authorGoff, Randal D.en_US
dc.contributor.authorBingman, Craig A.en_US
dc.contributor.authorGrüschow, Sabineen_US
dc.contributor.authorSherman, David H.en_US
dc.contributor.authorPhillips, George N.en_US
dc.contributor.authorThorson, Jon S.en_US
dc.date.accessioned2011-11-10T15:36:43Z
dc.date.available2012-09-04T15:27:45Zen_US
dc.date.issued2011-07en_US
dc.identifier.citationSingh, Shanteri; Chang, Aram; Goff, Randal D.; Bingman, Craig A.; Grüschow, Sabine ; Sherman, David H.; Phillips, George N.; Thorson, Jon S. (2011). "Structural characterization of the mitomycin 7â O â methyltransferase." Proteins: Structure, Function, and Bioinformatics 79(7): 2181-2188. <http://hdl.handle.net/2027.42/87038>en_US
dc.identifier.issn0887-3585en_US
dc.identifier.issn1097-0134en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/87038
dc.description.abstractMitomycins are quinone‐containing antibiotics, widely used as antitumor drugs in chemotherapy. Mitomycin‐7‐ O ‐methyltransferase (MmcR), a key tailoring enzyme involved in the biosynthesis of mitomycin in Streptomyces lavendulae , catalyzes the 7‐ O ‐methylation of both C9β‐ and C9α‐configured 7‐hydroxymitomycins. We have determined the crystal structures of the MmcR– S ‐adenosylhomocysteine (SAH) binary complex and MmcR–SAH–mitomycin A (MMA) ternary complex at resolutions of 1.9and 2.3 Å, respectively. The study revealed MmcR to adopt a common S ‐adenosyl‐ L ‐methionine‐dependent O ‐methyltransferase fold and the presence of a structurally conserved active site general acid–base pair is consistent with a proton‐assisted methyltransfer common to most methyltransferases. Given the importance of C7 alkylation to modulate mitomycin redox potential, this study may also present a template toward the future engineering of catalysts to generate uniquely bioactive mitomycins. Proteins 2011. © 2011 Wiley‐Liss, Inc.en_US
dc.publisherWiley Subscription Services, Inc., A Wiley Companyen_US
dc.subject.otherMethyltransferaseen_US
dc.subject.otherNatural Producten_US
dc.subject.otherMitomycinen_US
dc.subject.otherBiosynthesisen_US
dc.subject.otherS ‐Adenosyl‐ L ‐Methionineen_US
dc.subject.otherCanceren_US
dc.subject.otherX‐Ray Crystallographyen_US
dc.titleStructural characterization of the mitomycin 7‐ O ‐methyltransferaseen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumLife Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109‐2216en_US
dc.contributor.affiliationumDepartment of Medicinal Chemistry, University of Michigan, Ann Arbor, Michigan 48109‐2216en_US
dc.contributor.affiliationotherDivision of Pharmaceutical Sciences, Wisconsin Center for Natural Product Research, School of Pharmacy, University of Wisconsin‐Madison, Madison, Wisconsin 53705en_US
dc.contributor.affiliationotherDepartment of Biochemistry, University of Wisconsin‐Madison, Madison, Wisconsin 53706en_US
dc.contributor.affiliationotherDepartment of Biochemistry, University of Wisconsin‐Madison, Madison, WI 53706en_US
dc.contributor.affiliationotherDivision of Pharmaceutical Sciences, Wisconsin Center for Natural Product Research, School of Pharmacy, University of Wisconsin‐Madison, Madison, WI 53705en_US
dc.identifier.pmid21538548en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/87038/1/PROT_23040_sm_suppinfo.pdf
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/87038/2/23040_ftp.pdf
dc.identifier.doi10.1002/prot.23040en_US
dc.identifier.sourceProteins: Structure, Function, and Bioinformaticsen_US
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dc.owningcollnameInterdisciplinary and Peer-Reviewed


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