000064349 001__ 64349
000064349 005__ 20190709135703.0
000064349 0247_ $$2doi$$a10.1073/pnas.1713698114
000064349 0248_ $$2sideral$$a103549
000064349 037__ $$aART-2017-103549
000064349 041__ $$aeng
000064349 100__ $$aBuey, R.M.
000064349 245__ $$aUnprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase
000064349 260__ $$c2017
000064349 5060_ $$aAccess copy available to the general public$$fUnrestricted
000064349 5203_ $$aFlavoproteins participate in a wide variety of physiologically relevant processes that typically involve redox reactions. Within this protein superfamily, there exists a group that is able to transfer reducing equivalents from FAD to a redox-active disulfide bridge, which further reduces disulfide bridges in target proteins to regulate their structure and function. We have identified a previously undescribed type of flavin enzyme that is exclusive to oxygenic photosynthetic prokaryotes and that is based on the primary sequence that had been assigned as an NADPH-dependent thioredoxin reductase (NTR). However, our experimental data show that the protein does not transfer reducing equivalents from flavins to disulfides as in NTRs but functions in the opposite direction. High-resolution structures of the protein from Gloeobacter violaceus and Synechocystis sp. PCC6803 obtained by X-ray crystallography showed two juxtaposed FAD molecules per monomer in redox communication with an active disulfide bridge in a variant of the fold adopted by NTRs. We have tentatively named the flavoprotein “DDOR” (diflavin-linked disulfide oxidoreductase) and propose that its activity is linked to a thiol-based transfer of reducing equivalents in bacterial membranes. These findings expand the structural and mechanistic repertoire of flavoenzymes with oxidoreductase activity and pave the way to explore new protein engineering approaches aimed at designing redox-active proteins for diverse biotechnological applications.
000064349 536__ $$9info:eu-repo/grantAgreement/ES/MINECO/BIO2016-75634-P$$9info:eu-repo/grantAgreement/ES/MINECO/BFU2016-80343-P$$9info:eu-repo/grantAgreement/EC/FP7/283570/EU/Transnational access and enhancement of integrated Biological Structure determination at synchrotron X-ray radiation facilities/BIOSTRUCT-X
000064349 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
000064349 590__ $$a9.504$$b2017
000064349 591__ $$aMULTIDISCIPLINARY SCIENCES$$b5 / 64 = 0.078$$c2017$$dQ1$$eT1
000064349 592__ $$a6.092$$b2017
000064349 593__ $$aMultidisciplinary$$c2017$$dQ1
000064349 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000064349 700__ $$aArellano, J.B.
000064349 700__ $$aLópez-Maury, L.
000064349 700__ $$aGalindo-Trigo, S.
000064349 700__ $$0(orcid)0000-0001-5702-4538$$aVelázquez-Campoy, A.$$uUniversidad de Zaragoza
000064349 700__ $$aRevuelta, J.L.
000064349 700__ $$aDe Pereda, J.M.
000064349 700__ $$aFlorencio, F.J.
000064349 700__ $$aSchürmann, P.
000064349 700__ $$aBuchanan, B.B.
000064349 700__ $$aBalsera, M.
000064349 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000064349 773__ $$g114, 48 (2017), 12725-12730$$pProc. Natl. Acad. Sci.$$tProceedings of the National Academy of Sciences$$x0027-8424
000064349 8564_ $$s1229445$$uhttps://zaguan.unizar.es/record/64349/files/texto_completo.pdf$$yVersión publicada
000064349 8564_ $$s147955$$uhttps://zaguan.unizar.es/record/64349/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000064349 909CO $$ooai:zaguan.unizar.es:64349$$particulos$$pdriver
000064349 951__ $$a2019-07-09-12:50:52
000064349 980__ $$aARTICLE