@article {16921, title = {Tripartite binding mode of cohesin-dockerin complexes from Ruminococcus flavefaciens involving naturally truncated dockerins}, volume = {301}, year = {2025}, note = {n/a}, month = {2025}, pages = {110325}, abstract = {

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.

}, keywords = {Carbohydrates, cellulosome, cohesin, dockerin, protein assembly, protein complex, protein structure}, isbn = {0021-9258}, url = {https://www.sciencedirect.com/science/article/pii/S0021925825021751}, author = {Marlene Duarte and Carvalho, Ana Lu{\'\i}sa and Ferreira, Magda C. and Caires, Beatriz and Rom{\~a}o, Maria Jo{\~a}o and Prates, Jos{\'e} A. M. and Najmudin, Shabir and Bayer, Edward A. and Fontes, Carlos MGA. and Bule, Pedro} } @inbook {10.1039/9781788010641-00159, title = {Targeting protein-carbohydrate interactions in plant cell-wall biodegradation: the power of carbohydrate microarrays}, booktitle = {Carbohydrate Chemistry: Chemical and Biological Approaches Volume 43}, volume = {43}, year = {2018}, note = {n/a}, pages = {159-176}, publisher = {The Royal Society of Chemistry}, organization = {The Royal Society of Chemistry}, 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.

}, isbn = {978-1-78801-003-0}, doi = {10.1039/9781788010641-00159}, url = {http://dx.doi.org/10.1039/9781788010641-00159}, author = {Ribeiro, Diana O. and Pinheiro, Benedita A. and Carvalho, Ana Luisa and Palma, Angelina S.} } @article {Kryshtafovych2017, title = {Target highlights from the first post-PSI CASP experiment (CASP12, May-August 2016)}, journal = {Proteins: Structure, Function, and Bioinformatics}, year = {2017}, note = {

n/a

}, month = {oct}, abstract = {

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.

}, keywords = {CASP, NMR, protein structure prediction, X-ray crystallography}, issn = {08873585}, doi = {10.1002/prot.25392}, url = {http://www.ncbi.nlm.nih.gov/pubmed/28960539 http://doi.wiley.com/10.1002/prot.25392}, author = {Kryshtafovych, Andriy and Albrecht, Reinhard and Basl{\'e}, Arnaud and Bule, Pedro and Caputo, Alessandro T. and Carvalho, Ana Luisa and Chao, Kinlin L. and Diskin, Ron and Fidelis, Krzysztof and Fontes, Carlos M. G. A. and Fredslund, Folmer and Gilbert, Harry J. and Goulding, Celia W. and Hartmann, Marcus D. and Hayes, Christopher S. and Herzberg, Osnat and Hill, Johan C. and Joachimiak, Andrzej and Kohring, Gert-Wieland and Koning, Roman I. and {Lo Leggio}, Leila and Mangiagalli, Marco and Michalska, Karolina and Moult, John and Najmudin, Shabir and Nardini, Marco and Nardone, Valentina and Ndeh, Didier and Nguyen, Thanh H. and Pintacuda, Guido and Postel, Sandra and van Raaij, Mark J. and Roversi, Pietro and Shimon, Amir and Singh, Abhimanyu K. and Sundberg, Eric J. and Tars, Kaspars and Zitzmann, Nicole and Schwede, Torsten} } @article {Hussain2017, title = {Tunable gas sensing gels by cooperative assembly}, journal = {Advanced Functional Materials}, volume = {just accep}, number = {xx}, year = {2017}, note = {

n/a

}, month = {may}, pages = {xx}, abstract = {

n/a

}, keywords = {gas sensing, gelatin, ionic liquids, liquid crystals, self-assembly}, issn = {1616301X}, doi = {10.1002/adfm.201700803}, url = {http://doi.wiley.com/10.1002/adfm.201700803}, author = {Hussain, Abid and Semeano, Ana T. S. and Palma, Susana I.C.J. and Pina, Ana S. and Almeida, Jos{\'e} and Medrado, B{\'a}rbara F. and P{\'a}dua, Ana C. C. S. and Carvalho, Ana L. and Dion{\'\i}sio, Madalena and Li, Rosamaria W. C. and Gamboa, Hugo and Ulijn, Rein V. and Gruber, Jonas and Roque, Ana C. A.} }