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Open AccessJournal ArticleDOI

Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 å resolution

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TLDR
The determination of the structure of this protein provides fundamental knowledge for understanding its mode of action and the nature of allosteric conformational changes that regulate its function.
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This article is published in Structure.The article was published on 1995-12-01 and is currently open access. It has received 77 citations till now. The article focuses on the topics: Allosteric enzyme & Glucose phosphate.

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CH–π hydrogen bonds in biological macromolecules

TL;DR: The present Perspective will show the importance of CH-π hydrogen bonds and stimulate interest in the interactions of biological macromolecules, one of the most fascinating fields in bioorganic chemistry.
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An electrostatic/hydrogen bond switch as the basis for the specific interaction of phosphatidic acid with proteins.

TL;DR: It is demonstrated that this electrostatic/hydrogen bond switch turns the phosphate of PA into an effective and preferred docking site for lysine and arginine residues, and PA may well be nature's preferred membrane lipid for interfacial insertion of positively charged membrane protein domains.
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Controlling Allosteric Networks in Proteins.

TL;DR: A synergistic computational and experimental approach to rescue the cystic-fibrosis-associated protein cystic fibrosis transmembrane conductance regulator is described, which upon deletion of a single residue misfolds and causes disease.
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Refolding chromatography with immobilized mini-chaperones

TL;DR: Refolding chromatography offers an efficient and simple means to renature proteins in high yield and with biological activity.
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Controlling allosteric networks in proteins

TL;DR: In this article, the physical and evolutionary origin of protein allostery is discussed, as well as its importance to protein regulation, drug discovery, and biological processes in living systems.
References
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Journal ArticleDOI

The CCP4 suite: programs for protein crystallography

TL;DR: The CCP4 (Collaborative Computational Project, number 4) program suite is a collection of programs and associated data and subroutine libraries which can be used for macromolecular structure determination by X-ray crystallography.
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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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On the Nature of Allosteric Transitions: A Plausible Model

TL;DR: "It is certain that all bodies whatsoever, though they have no sense, yet they have perception, and whether the body be alterant or alterec, evermore a perception precedeth operation; for else all bodies would be like one to another."
Book

Introduction to protein structure

TL;DR: Part 1 BASIC STRUCTURAL PRINCIPLES: The Building Blocks and Motifs of Protein Structure and Part 2 STRUCTURE, FUNCTION and ENGINEERING: Structure, Function and Engineering.
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WHAT IF: A molecular modeling and drug design program

TL;DR: The menu-driven operation of WHAT IF, combined with the use of default values wherever user input is required, makes it very easy to use for a novice user while keeping full flexibility for more sophisticated studies.
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