Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release - Wikidata - awgldk - TriplyDB

Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release

Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release

http://www.wikidata.org/entity/Q34133375

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Solution Structure of the 128 kDa Enzyme I Dimer from Escherichia coli and Its 146 kDa Complex with HPr Using Residual Dipolar Couplings and Small- and Wide-Angle X-ray Scattering A conformational switch underlies ClpP protease function Solution structure of a minor and transiently formed state of a T4 lysozyme mutant Structural Switching of Staphylococcus aureus Clp Protease: A KEY TO UNDERSTANDING PROTEASE DYNAMICS Structural Insights into the Inactive Subunit of the Apicoplast-localized Caseinolytic Protease Complex of Plasmodium falciparum Structural insights into the conformational diversity of ClpP from Bacillus subtilis Structural model for the protein-translocating element of the twin-arginine transport system Insights into Structural Network Responsible for Oligomerization and Activity of Bacterial Virulence Regulator Caseinolytic Protease P (ClpP) Protein Helix Unfolding/Refolding Characterizes the Functional Dynamics of Staphylococcus aureus Clp Protease Protein structure determination from NMR chemical shifts The application of FAST-NMR for the identification of novel drug discovery targets Advances in Nuclear Magnetic Resonance for Drug Discovery.Role of a conserved pore residue in the formation of a prehydrolytic high substrate affinity state in the AAA+ chaperone ClpA Structural basis underlying the dual gate properties of KcsA Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.The ClpP N-terminus coordinates substrate access with protease active site reactivity.ClpXP, an ATP-powered unfolding and protein-degradation machine AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.Engineering of an epoxide hydrolase for efficient bioresolution of bulky pharmaco substrates.An introduction to NMR-based approaches for measuring protein dynamics.A cost-effective protocol for the parallel production of libraries of 13CH3-specifically labeled mutants for NMR studies of high molecular weight proteins.Flexible stoichiometry and asymmetry of the PIDDosome core complex by heteronuclear NMR spectroscopy and mass spectrometry.A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase.Allosteric cooperativity in protein kinase A.Automated assignment in selectively methyl-labeled proteins.Solution NMR of large molecules and assemblies ClpP: a distinctive family of cylindrical energy-dependent serine proteases.NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.The structural dynamics of macromolecular processes.NMR spectroscopy brings invisible protein states into focus.NMR reveals novel mechanisms of protein activity regulation.Dynamics of the ClpP serine protease: a model for self-compartmentalized proteases.Escherichia coli Quorum-Sensing EDF, A Peptide Generated by Novel Multiple Distinct Mechanisms and Regulated by trans-Translation.Longitudinal exchange: an alternative strategy towards quantification of dynamics parameters in ZZ exchange spectroscopy Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Mini review: ATP-dependent proteases in bacteria.Protein dynamics and function from solution state NMR spectroscopy.The Rrp4-exosome complex recruits and channels substrate RNA by a unique mechanism.The oligomeric architecture of the archaeal exosome is important for processive and efficient RNA degradation.An excess of catalytically required motions inhibits the scavenger decapping enzyme.

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Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release

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Anna Gribun

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Peter M Hwang

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Remco Sprangers

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Walid A Houry

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Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Crystal structure of ClpX molecular chaperone from Helicobacter pylori

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

Structure of 20S proteasome from yeast at 2.4 A resolution

Crystal structure of heat shock locus V (HslV) from Escherichia coli

The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle.

NMR analysis of a 900K GroEL GroES complex

Proteasomes and their kin: proteases in the machine age

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