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The crystal structure of the bacterial chaperonin GroEL at 2.8 A.

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TLDR
The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry.
Abstract
The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits consist of three domains: a large equatorial domain that forms the foundation of the assembly at its waist and holds the rings together; a large loosely structured apical domain that forms the ends of the cylinder; and a small slender intermediate domain that connects the two, creating side windows. The three-dimensional structure places most of the mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder.

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Citations
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Journal ArticleDOI

Molecular chaperones in cellular protein folding.

TL;DR: Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.
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The Hsp70 and Hsp60 chaperone machines.

TL;DR: This work dedicates this work to Guenter Brueckner, always an inspiration, and to Wayne Fenton for critical reading and Zhaohui Xu for figure preparation.
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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.

TL;DR: The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging.
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Automated molecular microscopy: the new Leginon system.

TL;DR: The primary automated data acquisition software system, Leginon, has been completely redesigned over the past two years and the system has demonstrated the capacity for high throughput data acquisition by acquiring images of more than 100,000 particles in a single session at the microscope.
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Absolute Quantification of Proteins by LCMSE A Virtue of Parallel ms Acquisition

TL;DR: A new method of absolute quantification of proteins is described, based on the discovery of an unexpected relationship between MS signal response and protein concentration, which is constant within a coefficient of variation of less than ±10%.
References
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Journal ArticleDOI

Improved methods for building protein models in electron density maps and the location of errors in these models.

TL;DR: In this paper, the authors describe strategies and tools that help to alleviate this problem and simplify the model-building process, quantify the goodness of fit of the model on a per-residue basis and locate possible errors in peptide and side-chain conformations.
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The interpretation of protein structures: estimation of static accessibility.

TL;DR: The accessibility of atoms in the twenty common amino acids in model tripeptides of the type Ala-X-Ala are given for defined conformation and the larger non-polar amino acids tend to be more “buried” in the native form of all three proteins.
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Protein folding in the cell.

TL;DR: Folding and assembly of polypeptides in vivo involves other proteins, many of which belong to families that have been highly conserved during evolution.
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Assessment of protein models with three-dimensional profiles.

TL;DR: It is shown that an effective test of the accuracy of a 3D protein model is a comparison of the model to its own amino-acid sequence, using a3D profile, computed from the atomic coordinates of the structure 3D profiles of correct protein structures match their own sequences with high scores, in contrast,3D profiles for protein models known to be wrong score poorly.
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Improved Fourier coefficients for maps using phases from partial structures with errors

TL;DR: In this article, a method is given to estimate the parameter σA in these phase probability expressions from the observed and calculated structure factor amplitudes, from which one can estimate the mean coordinate error for the model, and when there are coordinate errors, a new expression for the non-centric Fourier coefficients is required to suppress this model bias.
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