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Ribeiro, DO, Pinheiro BA, Carvalho AL, Palma AS.  2018.  Targeting protein-carbohydrate interactions in plant cell-wall biodegradation: the power of carbohydrate microarrays. Carbohydrate Chemistry: Chemical and Biological Approaches Volume 43. 43:159-176.: 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.

New book chapter!

Congratulations, Rita!

PhD student Ana Rita Otrelo Cardoso is at this moment defending her PhD thesis work entitled "Structural studies on molybdenum-dependent enzymes: from transporters to enzymes", co-supervised by Teresa Santos Silva and Maria João Romão. Well done, Rita! We're all very proud of your work!

Congrats, Diana!


Today, PhD student Diana Ribeiro publicly presented her PhD Workplan to the Thesis Advisory Committee. Congratulations, Diana, your thesis is in the right track!

Hussain, A, Semeano ATS, Palma SICJ, Pina AS, Almeida J, Medrado BF, Pádua ACCS, Carvalho AL, Dionísio M, Li RWC, Gamboa H, Ulijn RV, Gruber J, Roque ACA.  2017.  Tunable Gas Sensing Gels by Cooperative Assembly. Advanced Functional Materials. 27:1700803–n/a., Number 27 AbstractWebsite

The cooperative assembly of biopolymers and small molecules can yield functional materials with precisely tunable properties. Here, the fabrication, characterization, and use of multicomponent hybrid gels as selective gas sensors are reported. The gels are composed of liquid crystal droplets self-assembled in the presence of ionic liquids, which further coassemble with biopolymers to form stable matrices. Each individual component can be varied and acts cooperatively to tune gels' structure and function. The unique molecular environment in hybrid gels is explored for supramolecular recognition of volatile compounds. Gels with distinct compositions are used as optical and electrical gas sensors, yielding a combinatorial response conceptually mimicking olfactory biological systems, and tested to distinguish volatile organic compounds and to quantify ethanol in automotive fuel. The gel response is rapid, reversible, and reproducible. These robust, versatile, modular, pliant electro-optical soft materials possess new possibilities in sensing triggered by chemical and physical stimuli.

Kryshtafovych, A, Albrecht R, Baslé A, Bule P, Caputo AT, Carvalho AL, Chao KL, Diskin R, Fidelis K, Fontes CMGA, Fredslund F, Gilbert HJ, Goulding CW, Hartmann MD, Hayes CS, Herzberg O, Hill JC, Joachimiak A, Kohring G-W, Koning RI, {Lo Leggio} L, Mangiagalli M, Michalska K, Moult J, Najmudin S, Nardini M, Nardone V, Ndeh D, Nguyen TH, Pintacuda G, Postel S, van Raaij MJ, Roversi P, Shimon A, Singh AK, Sundberg EJ, Tars K, Zitzmann N, Schwede T.  2017.  Target highlights from the first post-PSI CASP experiment (CASP12, May-August 2016), oct. Proteins: Structure, Function, and Bioinformatics. 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.

New paper online!

Congrats, Frederico!

Today, our MSc student Frederico Lourenço defended his thesis entitled "Assignment of new roles for malectin-like domains to understand their divergent evolution". Congratulations to Frederico and his supervisor Benedita Pinheiro! All the best for future projects!

Maria João appointed Co-Editor of Acta F

Congratulations to our group leader Maria João Romão, who is now Co-editor of Acta Crystallographica Section F (Structural Biology Communications), appointed by the IUCr Executive Committee!
Maria João is now part of an excellent Editorial Board of renowned scientists.

This journal welcomes articles on relevant aspects of structural biology.

Congrats, Diogo!

Diogo Melo, MSc student supervised by Catarina Coelho and Maria João Romão, is right now defending his master's thesis! His research work is entitled “Structure based reaction mechanism studies on periplasmic nitrate reductase”. Congratulations and all the best for your future projects, Diogo!

At GLUPOR12

PhD student Diana Ribeiro presented her work on the functional and structural characterization of a new protein that binds to chitin. Well done, Diana!

At GLUPOR12

In her oral presentation, PhD student Viviana Correia described how she looks for new protein-glycan interactions of the human microbiome. Another successful talk!

At GLUPOR 12


Doctor Benedita Pinheiro presented her research results on the functional and structural characterization of a very important protein that plays a crucial role in the human endoplasmic reticulum. Congratulations, Benedita!

At the GLUPOR12

Raquel Costa and Frederico Lourenço are presenting their research work as poster communications at Glupor12, in Aveiro!

Polino, M, Carvalho AL, Juknaitė L, Portugal CAM, Coelhoso IM, Romão MJ, Crespo JG.  2017.  Ion-Exchange Membranes for Stable Derivatization of Protein Crystals, 2017. Crystal Growth & DesignCrystal Growth & Design. : American Chemical Society AbstractWebsite
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New paper online!

Ion-Exchange Membranes for Stable Derivatization of Protein Crystals

Otrelo-Cardoso, AR, Nair RR, Correia MAS, Cordeiro RCS, Panjkovich A, Svergun DI, Santos-Silva T, Rivas MG.  2017.  Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20, 2017. Scientific Reports. 7(1):5798. AbstractWebsite

Molybdenum and tungsten are taken up by bacteria and archaea as their soluble oxyanions through high affinity transport systems belonging to the ATP-binding cassette (ABC) transporters. The component A (ModA/TupA) of these transporters is the first selection gate from which the cell differentiates between MoO4 2−, WO4 2− and other similar oxyanions. We report the biochemical characterization and the crystal structure of the apo-TupA from Desulfovibrio desulfuricans G20, at 1.4 Å resolution. Small Angle X-ray Scattering data suggests that the protein adopts a closed and more stable conformation upon ion binding. The role of the arginine 118 in the selectivity of the oxyanion was also investigated and three mutants were constructed: R118K, R118E and R118Q. Isothermal titration calorimetry clearly shows the relevance of this residue for metal discrimination and oxyanion binding. In this sense, the three variants lost the ability to coordinate molybdate and the R118K mutant keeps an extremely high affinity for tungstate. These results contribute to an understanding of the metal-protein interaction, making it a suitable candidate for a recognition element of a biosensor for tungsten detection.

New paper online!

Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
Ana Rita Otrelo-Cardoso, Rashmi R. Nair, Márcia A. S. Correia, Raquel S. Correia Cordeiro, Alejandro Panjkovich, Dmitri I. Svergun, Teresa Santos-Silva & Maria G. Rivas 

Maria João Romão elected member of the Faculty's Council

Congratulations to Maria João and the other new members of the Faculty's Council, elected yesterday!

If you want to know more about the FCT-NOVA Council's duties: http://www.cf.fct.unl.pt

Romão, MJ, Coelho C, Santos-Silva T, Foti A, Terao M, Garattini E, Leimkühler S.  2017.  Structural basis for the role of mammalian aldehyde oxidases in the metabolism of drugs and xenobiotics. Current Opinion in Chemical Biology. 37:39-47. AbstractWebsite

Aldehyde oxidases (AOXs) are molybdo-flavoenzymes characterized by broad substrate specificity, oxidizing aromatic/aliphatic aldehydes into the corresponding carboxylic acids and hydroxylating various heteroaromatic rings. Mammals are characterized by a complement of species-specific \{AOX\} isoenzymes, that varies from one in humans (AOX1) to four in rodents (AOX1, AOX2, \{AOX3\} and AOX4). The physiological function of mammalian \{AOX\} isoenzymes is unknown, although human \{AOX1\} is an emerging enzyme in phase-I drug metabolism. Indeed, the number of therapeutic molecules under development which act as \{AOX\} substrates is increasing. The recent crystallization and structure determination of human \{AOX1\} as well as mouse \{AOX3\} has brought new insights into the mechanisms underlying substrate/inhibitor binding as well as the catalytic activity of this class of enzymes.