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.
Mukhopadhyay, A, Kladova AV, Bursakov SA, Gavel YO, Calvete JJ, Shnyrov VL, Moura I, Moura JJG, Romao MJ, Trincao J.
2011.
Crystal structure of the zinc-, cobalt-, and iron-containing adenylate kinase from Desulfovibrio gigas: a novel metal-containing adenylate kinase from Gram-negative bacteria. Journal of Biological Inorganic Chemistry. 16:51-61., Number 1
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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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Archer, M, Huber R, Tavares P, Moura I, Moura JJG, Carrondo MA, Sieker LC, Legall J, Romao MJ.
1995.
CRYSTAL-STRUCTURE OF DESULFOREDOXIN FROM DESULFOVIBRIO-GIGAS DETERMINED AT 1.8 ANGSTROM RESOLUTION - A NOVEL NONHEME IRON PROTEIN-STRUCTURE. Journal of Molecular Biology. 251:690-702., Number 5
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Romao, MJ, Archer M, Moura I, Moura JJG, Legall J, Engh R, Schneider M, Hof P, Huber R.
1995.
CRYSTAL-STRUCTURE OF THE XANTHINE OXIDASE-RELATED ALDEHYDE OXIDOREDUCTASE FROM D-GIGAS. Science. 270:1170-1176., Number 5239
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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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