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Prediction of the structure of GroES and its interaction with GroEL
Author(s) -
Valencia Alfonso,
Hubbard Tim J.,
Muga Arturo,
Bañuelos Sonia,
Llorca Oscar,
Carrascosa José L.,
Valpuesta José Marí
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340220302
Subject(s) - groel , groes , antiparallel (mathematics) , monomer , crystallography , beta (programming language) , fourier transform , chemistry , nuclear magnetic resonance , materials science , molecular physics , physics , polymer , biochemistry , computer science , quantum mechanics , escherichia coli , magnetic field , gene , programming language
Abstract The three‐dimensional structure of the GroES monomer and its interaction with GroEL has been predicted using a combination of prediction tools and experimental data obtained by biophysical [electron microscope (EM), Fourier transform infrared (FTIR), and nuclear magnetic resonance (NMR)] and biochemical techniques. The GroES monomer, according to the prediction, is composed of eight β‐strands forming a β‐barrel with loose ends. In the model, β‐strands 5–8 run along the outer surface of GroES, forming an antiparallel β‐sheet with β4 loosely bound to one of the edges. β‐strands 1–3 would then be parallel and placed in the interior of the molecule. Loops 1–3 would face the internal cavity of the GroEL–GroES complex, and together with conserved residues in loops 5 and 7, would form the active surface interacting with GroEL. © 1995 Wiley‐Liss, Inc.