2016
DOI: 10.1074/jbc.m116.761643
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Single Binding Mode Integration of Hemicellulose-degrading Enzymes via Adaptor Scaffoldins in Ruminococcus flavefaciens Cellulosome

Abstract: Edited by Gerald HartThe assembly of one of Nature's most elaborate multienzyme complexes, the cellulosome, results from the binding of enzymeborne dockerins to reiterated cohesin domains located in a noncatalytic primary scaffoldin. Generally, dockerins present two similar cohesin-binding interfaces that support a dual binding mode. The dynamic integration of enzymes in cellulosomes, afforded by the dual binding mode, is believed to incorporate additional flexibility in highly populated multienzyme complexes.… Show more

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Cited by 21 publications
(17 citation statements)
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“…Based on primary sequence similarity, R. flavefaciens dockerins are classified in different groups. Recent studies have shown that groups 3 and 6 R. flavefaciens Docs display a single‐binding mode for their target Cohs, that is, binding occurs in one orientation only . Intriguingly, Group 1 Docs also do not seem to possess the internal sequence symmetry required to support the dual‐binding mode.…”
Section: Resultsmentioning
confidence: 99%
“…Based on primary sequence similarity, R. flavefaciens dockerins are classified in different groups. Recent studies have shown that groups 3 and 6 R. flavefaciens Docs display a single‐binding mode for their target Cohs, that is, binding occurs in one orientation only . Intriguingly, Group 1 Docs also do not seem to possess the internal sequence symmetry required to support the dual‐binding mode.…”
Section: Resultsmentioning
confidence: 99%
“…flavefaciens ScaC group 3 Coh (ref. 12 ; Figure S2 ). The structure of Rf CohScaB3, whether unbound or in complex with Rf Doc1a, was essentially identical (rmsd ~0.37 Å).…”
Section: Resultsmentioning
confidence: 99%
“…This contrasts with the interface of the recently described R . flavefaciens Rf CohScaC-Doc3 complex where the two Doc3 helices (helix 1 and helix 3) make similar contributions to CohScaC recognition 12 . In Rf CohScaC-Doc3, CohScaC’s α-helix located between β-strands 4 and 5, which is absent in Rf CohScaB3 and Rf CohScaA , is elevated in relation to the 8-3-6-5 plane allowing the entire Coh surface to be in closer proximity to both Doc α-helices.…”
Section: Resultsmentioning
confidence: 99%
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“…Curiosamente, a cohesina de ScaC se situa mais próxima a cohesinas de tipo-I nas árvores de filogenia, a despeito de suas semelhanças funcionais e estruturais com o tipo-II. 13 Existem ainda algumas estruturas disponíveis de cohesinas de tipo-III desacompanhadas de dockerinas, com outras peculiaridades, que corroboram a inexistência de um consenso com relação a características do tipo III, visto que há uma diferença grande de similaridade entre seus membros. Nas 223 dockerinas de FD-1 essa similaridade varia de 20 a 98%.…”
Section: Cohesinas E Dockerinas: Os Componentes Centrais Do Celulossomounclassified