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dc.contributor.authorEdeling, MA
dc.contributor.authorGuddat, LW
dc.contributor.authorFabianek, RA
dc.contributor.authorThony-Meyer, L
dc.contributor.authorMartin, JL
dc.date.accessioned2017-10-05T01:35:08Z
dc.date.available2017-10-05T01:35:08Z
dc.date.issued2002
dc.identifier.issn0969-2126
dc.identifier.doi10.1016/S0969-2126(02)00794-3
dc.identifier.urihttp://hdl.handle.net/10072/347889
dc.description.abstractCcmG is unlike other periplasmic thioredoxin (TRX)-like proteins in that it has a specific reducing activity in an oxidizing environment and a high fidelity of interaction. These two unusual properties are required for its role in c-type cytochrome maturation. The crystal structure of CcmG reveals a modified TRX fold with an unusually acidic active site and a groove formed from two inserts in the fold. Deletion of one of the groove-forming inserts disrupts c-type cytochrome formation. Two unique structural features of CcmG—an acidic active site and an adjacent groove—appear to be necessary to convert an indiscriminately binding scaffold, the TRX fold, into a highly specific redox protein.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherCell Press
dc.relation.ispartofpagefrom973
dc.relation.ispartofpageto979
dc.relation.ispartofissue7
dc.relation.ispartofjournalStructure
dc.relation.ispartofvolume10
dc.subject.fieldofresearchChemical sciences
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchBiochemistry and cell biology not elsewhere classified
dc.subject.fieldofresearchInformation and computing sciences
dc.subject.fieldofresearchcode34
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode310199
dc.subject.fieldofresearchcode46
dc.titleStructure of CcmG/DsbE at 1.14 Å resolution: High-fidelity reducing activity in an indiscriminately oxidizing environment
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorMartin, Jennifer


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