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The dynamics of the catalytic site in small GTPases, variations on a common motif
Author(s) -
Kötting Carsten,
Gerwert Klaus
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.05.021
Subject(s) - gtpase , rab , small gtpase , catalysis , gtpase activating protein , chemistry , ran , biophysics , microbiology and biotechnology , biology , biochemistry , signal transduction , g protein
Small GTPases control many cellular processes. Their catalytic downregulation by GTPase activating proteins (GAP) is essential. Many structural models of GTPase·GAP complexes obtained by X‐ray structural analysis are available nowadays. They reveal important insights into the catalytic site and can suggest important catalytic residues. But this information is static. Time‐resolved FTIR spectroscopy can resolve the dynamics of the catalytic site at atomic detail. For the investigation of GAP catalyzed GTPase reactions of small GTPases, the order of events like the action of certain catalytic amino acids, bond breakages and protein conformational changes can be elucidated. This is elaborated for many small GTPases like Ras, Rap, Ran, Rho and Rab and their cognate GAPs. Variations on a common dynamic motif of the catalytic site of small GTPase will be presented.