Publications

Export 4 results:
Sort by: [ Author  (Desc)] Title Type Year
A B C D E F G H I J K L M N O P Q R S [T] U V W X Y Z   [Show ALL]
R
Ribeiro, Diana O., Benedita A. Pinheiro, Ana Luisa Carvalho, and Angelina S. Palma. "Targeting protein-carbohydrate interactions in plant cell-wall biodegradation: the power of carbohydrate microarrays." Carbohydrate Chemistry: Chemical and Biological Approaches Volume 43. Vol. 43. The Royal Society of Chemistry, 2018. 159-176. Abstract

The plant cell-wall is constituted by structurally diverse polysaccharides. The biodegradation of these is a crucial process for life sustainability. Cellulolytic microorganisms are highly efficient in this process by assembling modular architectures of carbohydrate-active enzymes with appended non-catalytic carbohydrate-binding modules (CBMs). Carbohydrate microarrays offer high-throughput and sensitive tools for uncovering carbohydrate-binding specificities of CBMs{,} which is pivotal to understand the function of these modules in polysaccharide biodegradation mechanisms. Features of this technology will be here briefly reviewed with highlights of microarray approaches to study plant-carbohydrates and CBM-carbohydrate interactions{,} along with an overview of plant polysaccharides and microorganisms strategies for their recognition.

K
Kryshtafovych, Andriy, Reinhard Albrecht, Arnaud Baslé, Pedro Bule, Alessandro T. Caputo, Ana Luisa Carvalho, Kinlin L. Chao, Ron Diskin, Krzysztof Fidelis, Carlos M. G. A. Fontes, Folmer Fredslund, Harry J. Gilbert, Celia W. Goulding, Marcus D. Hartmann, Christopher S. Hayes, Osnat Herzberg, Johan C. Hill, Andrzej Joachimiak, Gert-Wieland Kohring, Roman I. Koning, Leila {Lo Leggio}, Marco Mangiagalli, Karolina Michalska, John Moult, Shabir Najmudin, Marco Nardini, Valentina Nardone, Didier Ndeh, Thanh H. Nguyen, Guido Pintacuda, Sandra Postel, Mark J. van Raaij, Pietro Roversi, Amir Shimon, Abhimanyu K. Singh, Eric J. Sundberg, Kaspars Tars, Nicole Zitzmann, and Torsten Schwede. "Target highlights from the first post-PSI CASP experiment (CASP12, May-August 2016)." Proteins: Structure, Function, and Bioinformatics (2017). AbstractWebsite

The functional and biological significance of the selected CASP12 targets are described by the authors of the structures. The crystallographers discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submitted to the CASP12 experiment. This article is protected by copyright. All rights reserved.

H
Hussain, Abid, Ana T. S. Semeano, Susana I. C. J. Palma, Ana S. Pina, José Almeida, Bárbara F. Medrado, Ana C. C. S. Pádua, Ana L. Carvalho, Madalena Dionísio, Rosamaria W. C. Li, Hugo Gamboa, Rein V. Ulijn, Jonas Gruber, and Ana C. A. Roque. "Tunable gas sensing gels by cooperative assembly." Advanced Functional Materials. just accep (2017): xx. AbstractWebsite

n/a

D
Duarte, Marlene, Ana Luísa Carvalho, Magda C. Ferreira, Beatriz Caires, Maria João Romão, José A. M. Prates, Shabir Najmudin, Edward A. Bayer, Carlos MGA. Fontes, and Pedro Bule. "Tripartite binding mode of cohesin-dockerin complexes from Ruminococcus flavefaciens involving naturally truncated dockerins." 301.7 (2025): 110325. AbstractWebsite

Polysaccharides in plant cell walls serve as a rich carbon and energy source, yet their structural complexity presents a barrier to efficient degradation. To address this, anaerobic microorganisms like R. flavefaciens have developed sophisticated multi-enzyme complexes known as cellulosomes, which enable the efficient breakdown of these recalcitrant polysaccharides. These complexes are assembled through high-affinity interactions between cohesin (Coh) modules in scaffoldin proteins and dockerin (Doc) modules in cellulosomal enzymes. R. flavefaciens FD-1 harbors one of the most intricate cellulosomes described to date, comprising over 200 Doc-containing proteins encoded in its genome. Despite substantial research on this cellulosome, the role of a group of truncated but functional dockerins, known as group-2 Docs, remains unclear. In this study, we present a detailed structural and binding analysis of a Coh-Doc complex involving the cohesin from the cell-anchoring scaffoldin ScaE and a group-2 Doc that bears only one of the two Ca+2-coordinating loops that characterise the canonical Docs. Our findings reveal a novel tripartite binding mechanism, in which the cohesin can simultaneously bind two distinct dockerin units in three alternative conformations. This discovery provides new insights into the modular versatility of the R. flavefaciens cellulosome and sheds light on the mechanisms that enhance its efficiency in polysaccharide degradation.