φ value analysis of heterogeneity in pathways of allosteric transitions:: Evidence for parallel pathways of ATP-induced conformational changes in a GroEL ring

被引:19
作者
Horovitz, A [1 ]
Amir, A [1 ]
Danziger, O [1 ]
Kafri, G [1 ]
机构
[1] Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel
关键词
nested allostery; cooperativity; chaperonins;
D O I
10.1073/pnas.222303299
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
What are the mechanisms of ligand-induced allosteric transitions in proteins? A powerful method to characterize pathways and transition states of reactions is phi value analysis. A phi value is the ratio between the changes on a perturbation (e.g., mutation) in the activation and equilibrium free energies of a reaction. Here, phi value analysis is used to characterize the ATP-induced allosteric transitions of GroEL by using changes in ATP concentration as perturbations. GroEL consists of two stacked back-to-back heptameric rings that bind ATP with positive cooperativity within rings and negative cooperativity between rings. Evidence is presented for the existence of parallel pathways for the allosteric transition of each ring. In both allosteric transitions, there is an abrupt ATP-dependent switch from a pathway with ATP-binding sites in the transition state that are very similar to those of the initial T state (phi = 0) to a pathway with a phi value of approximate to0.3. The phi value procedure outlined here should be useful in mapping the energy landscape of allosteric transitions of other proteins.
引用
收藏
页码:14095 / 14097
页数:3
相关论文
共 26 条
[2]   THE CRYSTAL-STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8-ANGSTROM [J].
BRAIG, K ;
OTWINOWSKI, Z ;
HEGDE, R ;
BOISVERT, DC ;
JOACHIMIAK, A ;
HORWICH, AL ;
SIGLER, PB .
NATURE, 1994, 371 (6498) :578-586
[3]   APPLICATION OF LINEAR FREE-ENERGY RELATIONS TO PROTEIN CONFORMATIONAL-CHANGES - THE QUATERNARY STRUCTURAL-CHANGE OF HEMOGLOBIN [J].
EATON, WA ;
HENRY, ER ;
HOFRICHTER, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (10) :4472-4475
[4]   A kinetic mechanism for nicotinic acetylcholine receptors based on multiple allosteric transitions [J].
Edelstein, SJ ;
Schaad, O ;
Henry, E ;
Bertrand, D ;
Changeux, JP .
BIOLOGICAL CYBERNETICS, 1996, 75 (05) :361-379
[5]   SINGLE VERSUS PARALLEL PATHWAYS OF PROTEIN-FOLDING AND FRACTIONAL FORMATION OF STRUCTURE IN THE TRANSITION-STATE [J].
FERSHT, AR ;
ITZHAKI, LS ;
ELMASRY, N ;
MATTHEWS, JM ;
OTZEN, DE .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (22) :10426-10429
[6]   QUANTITATIVE-ANALYSIS OF STRUCTURE-ACTIVITY-RELATIONSHIPS IN ENGINEERED PROTEINS BY LINEAR FREE-ENERGY RELATIONSHIPS [J].
FERSHT, AR ;
LEATHERBARROW, RJ ;
WELLS, TNC .
NATURE, 1986, 322 (6076) :284-286
[7]   THE FOLDING OF AN ENZYME .1. THEORY OF PROTEIN ENGINEERING ANALYSIS OF STABILITY AND PATHWAY OF PROTEIN FOLDING [J].
FERSHT, AR ;
MATOUSCHEK, A ;
SERRANO, L .
JOURNAL OF MOLECULAR BIOLOGY, 1992, 224 (03) :771-782
[8]   Mapping the conformational wave of acetylcholine receptor channel gating [J].
Grosman, C ;
Zhou, M ;
Auerbach, A .
NATURE, 2000, 403 (6771) :773-776
[9]   CHEMICAL RELAXATION SPECTRA - CALCULATION OF RELAXATION TIMES FOR COMPLEX MECHANISMS [J].
HAMMES, GG ;
SCHIMMEL, PR .
JOURNAL OF PHYSICAL CHEMISTRY, 1966, 70 (07) :2319-&