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Margarida Archer Lab

Macromolecular Crystallography Unit

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In the Membrane Protein Crystallography Laboratory, we determine the three-dimensional structure of biological macromolecules. The laboratory is integrated in the Macromolecular Crystallography Unit.

Margarida Archer
Principal Investigador
PhD in 1999 in ITQB NOVA

Phone (+351) 214469762 | Extension 1762
Email archer@itqb.unl.pt | Lab website

 

Research Interests

Elucidation of structure as a mean of understanding function is the basic principle of structural biology.  Our main goal is the three-dimensional structure determination of proteins by X-ray Crystallography, which reveals their overall fold and architecture of the active sites at atomic level.

Membrane proteins play crucial roles in essential cellular processes of living organisms, comprising about one-third of all proteins. Despite this, our structural understanding has lagged behind that of their soluble counterparts. We are currently working with membrane proteins involved in cell wall synthesis, transport and signaling. Furthermore, we are also interested in proteins participating in catalytic and metabolic pathways and proteins which are potential targets for drug design.

We collaborate with various groups (from NOVA and other universities) so that our crystallographic analysis of the proteins, combined with other complementary methods, such as biochemical and biophysical experiments, may provide insides into their biological function and reaction mechanism. Our objective is a better understanding of protein structure-function relationship.

 

 Group Members

  • Margarida Archer, Head
  • José Brito, Post-doc
  • Márcia Alves, PhD student
  • José Rodrigues, PhD student
  • Diogo Athayde, Research student
  • Paulo Mamede, Master student

 

Selected Publications

  1. Nogly P, Gushchin I, Remeeva A, Esteves AM, Borges N, Ma P, Ishchenko A, Grudinin S, Round E, Moraes I, Borshchevskiy V, Santos H, Gordeliy V, Archer M. X-ray structure of a CDP-alcohol phosphatidyltransferase membrane enzyme and insights into catalytic mechanism. Nature Communic 5: 4169 (2014).

  2. Moraes I, Archer M. Methods for the successful crystallization of membrane proteins. Meth Mol Biol 1261: 211-230 (2015).

  3. Kurth JM, Brito JA, Reuter J, Flegler A, Koch T, Franke T, Klein EM, Rowe SF, Butt JN, Denkmann K, Pereira IA, Archer M, Dahl C. Electron Accepting Units of the Diheme Cytochrome c TsdA, a Bifunctional Thiosulfate Dehydrogenase/Tetrathionate Reductase. J Biol Chem 291: 24804-24818 (2016).

MX Unit Website

For further information please visit the MX Unit Website

 

Cristalografia de Proteínas Membranares (PT)

A elucidação da estrutura como meio para a compreensão da função é o princípio básico da biologia estrutural. O nosso principal objetivo é a determinação da estrutura tri-dimensional de proteínas por cristalografia de raios-x, que revela a sua estrutura global e arquitetura do centro ativo a nível atómico. As proteínas membranares desempenham papéis cruciais em processos celulares essenciais aos organismos, compreendendo cerca de um terço de todas as proteínas. Apesar disso, o nosso conhecimento estrutural destas proteínas é muito escasso quando comparado com as solúveis. Estamos atualmente a trabalhar com proteínas membranares envolvidas na síntese de parede celular, transporte e sinalização. Além disso, também estamos interessados em proteínas que participam em vias metabólicas e catalíticas e proteínas que são alvos para potenciais fármacos. Colaboramos com vários grupos (da NOVA e outras universidades), para que a análise cristalográfica das proteínas de interesse, combinado com outros métodos complementares, tais como ensaios bioquímicos e biofísicos, possam ajudar a uma melhor compreensão das suas funções biológicas e mecanismos de reação.

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