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Acta Crystallogr F Struct Biol Commun ; 76(Pt 2): 47-57, 2020 Feb 01.
Article in English | MEDLINE | ID: mdl-32039885

ABSTRACT

The structure of the MP-4 protein was previously determined at a resolution of 2.8 Å. Owing to the unavailability of gene-sequence information at the time, the side-chain assignment was carried out on the basis of a partial sequence available through Edman degradation, sequence homology to orthologs and electron density. The structure of MP-4 has now been determined at a higher resolution (2.22 Å) in another space group and all of the structural inferences that were presented in the previous report of the structure were validated. In addition, the present data allowed an improved assignment of side chains and enabled further analysis of the MP-4 structure, and the accuracy of the assignment was confirmed by the recently available gene sequence. The study reinforces the traditional concept that conservative interpretations of relatively low-resolution structures remain correct even with the availability of high-resolution data.


Subject(s)
Mucuna/metabolism , Plant Extracts/metabolism , Plant Proteins/chemistry , Protein Conformation , Seeds/chemistry , Amino Acid Sequence , Crystallography, X-Ray , Models, Molecular , Sequence Homology
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