De Schutter, A, Correia HD, Freire DM, Rivas MG, Rizzi A, Santos-Silva T, González PJ, Van Doorslaer S.
2015.
Ligand Binding to Chlorite Dismutase from Magnetospirillum sp, October. The journal of physical chemistry. B. 119:13859—13869., Number 43
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Dias, JM, Than ME, Huber R, Bourenkov GP, Bartunik HD, Bursakov S, Moura JJG, Moura I, Romao MJ.
1999.
Crystallographic studies of a dissimilatory nitrate reductase and mechanistic implications. Journal of Inorganic Biochemistry. 74:113-113., Number 1-4
Abstractn/a
Dias, JM, Than ME, Humm A, Huber R, Bourenkov GP, Bartunik HD, Bursakov S, Calvete J, Caldeira J, Carneiro C, Moura JJG, Moura I, Romao MJ.
1999.
Crystal structure of the first dissimilatory nitrate reductase at 1.9 angstrom solved by MAD methods. Structure with Folding & Design. 7:65-79., Number 1
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Dias, JM, Carvalho AL, Kolln I, Calvete JJ, TopferPetersen E, Varela PF, Romero A, Urbanke C, Romao MJ.
1997.
Crystallization and preliminary x-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture. Protein Science. 6:725-727., Number 3
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Dias, AMGC, Moreira IP, Lychko I, Lopes Soares C, Nurrito A, Moura Barbosa AJ, Lutz-Bueno V, Mezzenga R, Carvalho AL, Pina AS, Roque ACA.
2023.
Hierarchical self-assembly of a reflectin-derived peptide. Frontiers in Chemistry. 11
AbstractReflectins are a family of intrinsically disordered proteins involved in cephalopod camouflage, making them an interesting source for bioinspired optical materials. Understanding reflectin assembly into higher-order structures by standard biophysical methods enables the rational design of new materials, but it is difficult due to their low solubility. To address this challenge, we aim to understand the molecular self-assembly mechanism of reflectin’s basic unit—the protopeptide sequence YMDMSGYQ—as a means to understand reflectin’s assembly phenomena. Protopeptide self-assembly was triggered by different environmental cues, yielding supramolecular hydrogels, and characterized by experimental and theoretical methods. Protopeptide films were also prepared to assess optical properties. Our results support the hypothesis for the protopeptide aggregation model at an atomistic level, led by hydrophilic and hydrophobic interactions mediated by tyrosine residues. Protopeptide-derived films were optically active, presenting diffuse reflectance in the visible region of the light spectrum. Hence, these results contribute to a better understanding of the protopeptide structural assembly, crucial for the design of peptide- and reflectin-based functional materials.
Duarte, M, Viegas A, Alves VD, Prates JAM, Ferreira LMA, Najmudin S, Cabrita EJ, Carvalho AL, Fontes CMGA, Bule P.
2021.
A dual cohesin–dockerin complex binding mode in Bacteroides cellulosolvens contributes to the size and complexity of its cellulosome. Journal of Biological Chemistry. 296:100552.
AbstractThe Cellulosome is an intricate macromolecular protein complex that centralizes the cellulolytic efforts of many anaerobic microorganisms through the promotion of enzyme synergy and protein stability. The assembly of numerous carbohydrate processing enzymes into a macromolecular multiprotein structure results from the interaction of enzyme-borne dockerin modules with repeated cohesin modules present in noncatalytic scaffold proteins, termed scaffoldins. Cohesin–dockerin (Coh-Doc) modules are typically classified into different types, depending on structural conformation and cellulosome role. Thus, type I Coh-Doc complexes are usually responsible for enzyme integration into the cellulosome, while type II Coh-Doc complexes tether the cellulosome to the bacterial wall. In contrast to other known cellulosomes, cohesin types from Bacteroides cellulosolvens, a cellulosome-producing bacterium capable of utilizing cellulose and cellobiose as carbon sources, are reversed for all scaffoldins, i.e., the type II cohesins are located on the enzyme-integrating primary scaffoldin, whereas the type I cohesins are located on the anchoring scaffoldins. It has been previously shown that type I B. cellulosolvens interactions possess a dual-binding mode that adds flexibility to scaffoldin assembly. Herein, we report the structural mechanism of enzyme recruitment into B. cellulosolvens cellulosome and the identification of the molecular determinants of its type II cohesin–dockerin interactions. The results indicate that, unlike other type II complexes, these possess a dual-binding mode of interaction, akin to type I complexes. Therefore, the plasticity of dual-binding mode interactions seems to play a pivotal role in the assembly of B. cellulosolvens cellulosome, which is consistent with its unmatched complexity and size.