000060985 001__ 60985
000060985 005__ 20191105115759.0
000060985 0247_ $$2doi$$a10.1038/s41598-017-00402-6
000060985 0248_ $$2sideral$$a98608
000060985 037__ $$aART-2017-98608
000060985 041__ $$aeng
000060985 100__ $$aSerrano, A.$$uUniversidad de Zaragoza
000060985 245__ $$aThe trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes
000060985 260__ $$c2017
000060985 5060_ $$aAccess copy available to the general public$$fUnrestricted
000060985 5203_ $$aBifunctional FAD synthetases (FADSs) fold in two independent modules; The C-terminal riboflavin kinase (RFK) catalyzes the RFK activity, while the N-terminal FMN-adenylyltransferase (FMNAT) exhibits the FMNAT activity. The search for macromolecular interfaces in the Corynebacterium ammoniagenes FADS (CaFADS) crystal structure predicts a dimer of trimers organization. Within each trimer, a head-to-tail arrangement causes the RFK and FMNAT catalytic sites of the two neighboring protomers to approach, in agreement with active site residues of one module influencing the activity at the other. We analyze the relevance of the CaFADS head-to-tail macromolecular interfaces to stabilization of assemblies, catalysis and ligand binding. With this aim, we evaluate the effect of point mutations in loop L1c-FlapI, loop L6c, and helix a1c of the RFK module (positions K202, E203, F206, D298, V300, E301 and L304), regions at the macromolecular interface between two protomers within the trimer. Although none of the studied residues is critical in the formation and dissociation of assemblies, residues at L1c-FlapI and helix a1c particularly modulate quaternary architecture, as well as ligand binding and kinetic parameters involved with RFK and FMNAT activities. These data support the influence of transient oligomeric structures on substrate accommodation and catalysis at both CaFADS active sites.
000060985 536__ $$9info:eu-repo/grantAgreement/ES/DGA/B18$$9info:eu-repo/grantAgreement/ES/MICINN/BIO2013-42978-P$$9info:eu-repo/grantAgreement/ES/MINECO/BIO2016-75183-P
000060985 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000060985 590__ $$a4.122$$b2017
000060985 591__ $$aMULTIDISCIPLINARY SCIENCES$$b12 / 64 = 0.188$$c2017$$dQ1$$eT1
000060985 592__ $$a1.533$$b2017
000060985 593__ $$aMultidisciplinary$$c2017$$dQ1
000060985 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000060985 700__ $$0(orcid)0000-0001-7202-4587$$aSebastián, M.$$uUniversidad de Zaragoza
000060985 700__ $$aArilla-Luna, S.
000060985 700__ $$aBaquedano, S.
000060985 700__ $$0(orcid)0000-0003-2044-4795$$aHerguedas, B.
000060985 700__ $$0(orcid)0000-0001-5702-4538$$aVelázquez-Campoy, A.$$uUniversidad de Zaragoza
000060985 700__ $$0(orcid)0000-0001-9047-0046$$aMartínez-Júlvez, M.$$uUniversidad de Zaragoza
000060985 700__ $$0(orcid)0000-0001-8743-0182$$aMedina, M.$$uUniversidad de Zaragoza
000060985 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000060985 773__ $$g7 (2017), 404 [13 pp.]$$pSci. rep.$$tSCIENTIFIC REPORTS$$x2045-2322
000060985 8564_ $$s2682833$$uhttps://zaguan.unizar.es/record/60985/files/texto_completo.pdf$$yVersión publicada
000060985 8564_ $$s110397$$uhttps://zaguan.unizar.es/record/60985/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000060985 909CO $$ooai:zaguan.unizar.es:60985$$particulos$$pdriver
000060985 951__ $$a2019-11-05-11:50:06
000060985 980__ $$aARTICLE