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The Crystal Structures of Dihydropyrimidinases Reaffirm the Close Relationship between Cyclic Amidohydrolases and Explain Their Substrate Specificity

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TLDR
The extension of one of the sheets of the β-sandwich domain across a subunit-subunit interface in yeast dihydropyrimidinase underlines its closer evolutionary relationship to hydantoinases, whereas the slime mold enzyme shows higher similarity to the noncatalytic collapsin-response mediator proteins involved in neuron development.
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This article is published in Journal of Biological Chemistry.The article was published on 2006-05-12 and is currently open access. It has received 55 citations till now. The article focuses on the topics: Dihydropyrimidinase & Amidohydrolase.

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Journal ArticleDOI

The structure of human collapsin response mediator protein 2, a regulator of axonal growth.

TL;DR: The crystal structure of human tetrameric CRMP‐2 is determined, which is structurally related to the dihydropyriminidases; however, the active site is not conserved.
Journal ArticleDOI

The crystal structure of Escherichia coli TdcF, a member of the highly conserved YjgF/YER057c/UK114 family

TL;DR: The crystal structure of E. coli TdcF is determined and it is shown that TDCF is capable of binding several low molecular weight metabolites bearing a carboxylate group, although the interaction with 2-ketobutyrate appears to be the most well defined.
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Inhibition of a Putative Dihydropyrimidinase from Pseudomonas aeruginosa PAO1 by Flavonoids and Substrates of Cyclic Amidohydrolases.

TL;DR: This study was the first to demonstrate that naturally occurring product dihydromyricetin inhibited dihydropyrimidinase, even more than the substrate analogs (>3 orders of magnitude).
References
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Journal ArticleDOI

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
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Coot: model-building tools for molecular graphics.

TL;DR: CCP4mg is a project that aims to provide a general-purpose tool for structural biologists, providing tools for X-ray structure solution, structure comparison and analysis, and publication-quality graphics.
Journal ArticleDOI

PROCHECK: a program to check the stereochemical quality of protein structures

TL;DR: The PROCHECK suite of programs as mentioned in this paper provides a detailed check on the stereochemistry of a protein structure and provides an assessment of the overall quality of the structure as compared with well refined structures of the same resolution.
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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