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The structure of MP‐4 from Mucuna pruriens at 2.22 Å resolution
Author(s) -
Jain Abha,
Kumar Amit,
Shikhi Meha,
Kumar Ashish,
Nair Deepak T.,
Salunke Dinakar M.
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20000199
Subject(s) - mucuna pruriens , unavailability , sequence (biology) , resolution (logic) , edman degradation , low resolution , computational biology , homology modeling , computer science , algorithm , high resolution , mathematics , biology , genetics , gene , peptide sequence , artificial intelligence , statistics , biochemistry , geography , remote sensing , agronomy , enzyme
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.