(Q28145239)

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A dynamic model for the allosteric mechanism of GroEL

scientific article (publication date: 15 September 2000)

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A dynamic model for the allosteric mechanism of GroEL (English)

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4

M Karplus

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J Ma

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1

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P B Sigler

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2

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Z Xu

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English

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publication date

15 September 2000

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Journal of Molecular Biology

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302

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2

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303-13

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cites work

Structure and function in GroEL-mediated protein folding

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Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10

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On the relationship between the Hill coefficients for steady-state and transient kinetic data: a criterion for concerted transitions in allosteric proteins

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Mechanism of tertiary structural change in hemoglobin

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GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

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[24] Probing conformations of GroEL-bound substrate proteins by mass spectrometry

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GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism

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Conformational changes in the chaperonin GroEL: new insights into the allosteric mechanism

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GroEL-mediated protein folding

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GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps

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Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

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Molecular dynamics with coupling to an external bath

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Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

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Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

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Structural basis of allosteric changes in the GroEL mutant Arg197→Ala

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Residues in chaperonin GroEL required for polypeptide binding and release

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Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

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GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices

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Molecular switch in signal transduction: Reaction paths of the conformational changes in ras p21

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Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes

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The allosteric mechanism of the chaperonin GroEL: a dynamic analysis

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The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

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Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K dependent

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Molecular chaperones in protein folding and translocation

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GroEL/GroES: structure and function of a two-stroke folding machine

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Molecular chaperones in cellular protein folding

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Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

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A computational approach to simplifying the protein folding alphabet.

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The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

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Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state

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Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

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Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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Capturing the misfolds: chaperone-peptide-binding motifs.

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Protein folding Folding with a two-stroke motor

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Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL

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GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.

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Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

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Cooperativity in ATP hydrolysis by GroEL is increased by GroES

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A structural model for GroEL-polypeptide recognition

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Protein folding in the cell

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The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

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Identifiers

DOI

10.1006/JMBI.2000.4014

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2021221

OpenCitations bibliographic resource ID

2021221

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2021221

PubMed publication ID

10970735

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2021221

(Q28145239)

A dynamic model for the allosteric mechanism of GroEL

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