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Protein Engineering vol.10 no.2 pp.159167, 1997 Protein engineering with monomeric triosephosphate isomerase
 

Summary: peng$$0206
Protein Engineering vol.10 no.2 pp.159­167, 1997
Protein engineering with monomeric triosephosphate isomerase
(monoTIM): the modelling and structure verification of a seven-
residue loop
N.Thanki, J.Ph.Zeelen, M.Mathieu, R.Jaenicke1, ing experiments, in particular the design of new loops with
R.A.Abagyan2, R.K.Wierenga3 and W.Schliebs3 altered properties.
We have initiated a protein engineering project which is
EMBL, Postfach 102209, D69012 Heidelberg, 1Institut fušr Biophysik und aimed at redesigning the active site loops of TIM. TIM is a
Physikalische Biochemie, Universitašt Regensburg, Dg3040 Regensburg,
dimeric, glycolytic enzyme catalysing the interconversion ofGermany and 2The Skirball Institute for Biomolecular Medicine, New York
dihydroxyacetone phosphate and D-glyceraldehyde-3-phos-University, New York, NY 10016, USA
phate (Knowles, 1991). The catalytic residues of TIM are3To whom correspondence should be addressed
Lys13 (loop-1), His95 (loop-4) and Glu167 (loop-6), when
Protein engineering experiments have been carried out using the numbering scheme of trypanosomal TIM (Noble
with loop-1 of monomeric triosephosphate isomerase et al., 1993). In addition, in wild-type TIM loops-1­4 are
(monoTIM). Loop-1 of monoTIM is disordered in every involved in tight interactions across the dimer interface;
crystal structure of liganded monoTIM, but in the wild- consequently, these loops are very rigid in the wild-type dimer.
type TIM it is a very rigid dimer interface loop. This loop Our first design experiment was the monomerization of dimeric
connects the first -strand with the first -helix of the trypanosomal TIM. This was achieved by replacing the major

  

Source: Abagyan, Ruben - School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego

 

Collections: Biology and Medicine