Analysis of sequence information, structural and evolutionary protein superfamilies. Application to the enolase superfamily

MARTÍN BANCHERO; ELIN TEPPA; CRISTINA MARINO BUSLJE

Rosario

Congreso; 4to. Congreso Argentino de Bioinformática y Biología Computacional (4CAB2C) y 4ta. Conferencia Internacional de la Sociedad Iberoamericana de Bioinformática (SolBio); 2013

Asociación Argentina de Bioinformática y Biología Computacional and Sociedad Iberoamericana de Bioinformática

One of the most important and widely studied problems inprotein sequence analysis is identifying which residues in aprotein are responsible for its function.Enolase superfamily proteins shows a TIM-Barrel superfold,this fold is ubiquitous in all kingdoms of life and is one of themost frequently observed. Although families differ in theirfunction, specificity and even presents different reactionmechanisms, these enzymes share a common catalytic stepof abstraction of the alpha-proton of a carboxylate anion[1].Mutations of essential residues in a protein sequence mayoccur, only if a compensatory mutation takes placeelsewhere within the protein to preserve or restore activity[2]. These co-evolving mutations are of key interest sincethey identify residues that interact within the protein to carryout a particular function such as: catalytic reaction, structurestabilization, protein-protein and substrate interaction andallosteric regulation.