Chaves, S, Gil M, Canario S, Jelic R, Romao MJ, Trincao J, Herdtweck E, Sousa J, Diniz C, Fresco P, Santos AM.
2008.
Biologically relevant O,S-donor compounds. Synthesis, molybdenum complexation and xanthine oxidase inhibition. Dalton Transactions. :1773-1782., Number 13
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Carvalho, AL, Dias FMV, Prates JAM, Nagy T, Gilbert HJ, Davies GJ, Ferreira LMA, Romao MJ, Fontes C.
2003.
Cellulosome assembly revealed by the crystal structure of the cohesin-dockerin complex. Proceedings of the National Academy of Sciences of the United States of America. 100:13809-13814., Number 24
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Bursakov, SA, Brondino C, Dias JM, Carneiro C, Caldeira J, Duarte RO, Romao MJ, Moura I, Moura JJG.
1999.
Cross immunological reactions and spectroscopy study within nitrate reductase and other mononuclear Mo containing enzymes of the sulfate reducing bacteria. Journal of Inorganic Biochemistry. 74:86-86., Number 1-4
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Romao, MJ, Kolln I, Dias JM, Carvalho AL, Romero A, Varela PF, Sanz L, Topfer-Petersen E, Calvete JJ.
1997.
Crystal structure of acidic seminal fluid protein (aSFP) at 1.9 angstrom resolution: a bovine polypeptide of the spermadhesin family. Journal of Molecular Biology. 274:650-660., Number 4
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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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Gomes, AS, Trovão F, Andrade Pinheiro B, Freire F, Gomes S, Oliveira C, Domingues L, Romão MJ, Saraiva L, Carvalho AL.
2018.
The Crystal Structure of the R280K Mutant of Human p53 Explains the Loss of DNA Binding. International Journal of Molecular Sciences. 19, Number 4}, ARTICLE NUMBER = {1184
AbstractThe p53 tumor suppressor is widely found to be mutated in human cancer. This protein is regarded as a molecular hub regulating different cell responses, namely cell death. Compelling data have demonstrated that the impairment of p53 activity correlates with tumor development and maintenance. For these reasons, the reactivation of p53 function is regarded as a promising strategy to halt cancer. In the present work, the recombinant mutant p53R280K DNA binding domain (DBD) was produced for the first time, and its crystal structure was determined in the absence of DNA to a resolution of 2.0 Å. The solved structure contains four molecules in the asymmetric unit, four zinc(II) ions, and 336 water molecules. The structure was compared with the wild-type p53 DBD structure, isolated and in complex with DNA. These comparisons contributed to a deeper understanding of the mutant p53R280K structure, as well as the loss of DNA binding related to halted transcriptional activity. The structural information derived may also contribute to the rational design of mutant p53 reactivating molecules with potential application in cancer treatment.
Romero, A, Romao MJ, Varela PF, Kolln I, Dias JM, Carvalho AL, Sanz L, TopferPetersen E, Calvete JJ.
1997.
The crystal structures of two spermadhesins reveal the CUB domain fold. Nature Structural Biology. 4:783-788., Number 10
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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, 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
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Teixeira, S, Dias JM, Carvalho AL, Bourenkov G, Bartunik H, Almendra MJ, Moura I, Moura JJG, Romao MJ.
1999.
Crystallographic studies on a tungsten-containning formate dehydrogenase from Desulfovibrio gigas. Journal of Inorganic Biochemistry. 74:89-89., Number 1-4
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Cunha, CA, Macieira S, Dias JM, Almeida G, Goncalves LL, Costa C, Lampreia J, Huber R, Moura JJG, Moura I, Romao MJ.
2003.
Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774 - The relevance of the two calcium sites in the structure of the catalytic subunit (NrfA). Journal of Biological Chemistry. 278:17455-17465., Number 19
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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.
Carvalho, AL, Dias FMV, Nagy T, Prates JAM, Proctor MR, Smith N, Bayer EA, Davies GJ, Ferreira LMA, Romao MJ, Fontes CMGA, Gilbert HJ.
2007.
Evidence for a dual binding mode of dockerin modules to cohesins. Proceedings of the National Academy of Sciences of the United States of America. 104:3089-3094., Number 9
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