The structure of MP-4 from Mucuna pruriens at 2.22 Å resolution

Acta Crystallogr F Struct Biol Commun. 2020 Feb 1;76(Pt 2):47-57. doi: 10.1107/S2053230X20000199. Epub 2020 Feb 3.

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.

Keywords: MP-4; Mucuna pruriens; high resolution; plant proteins; protease inhibitors.

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Models, Molecular
  • Mucuna / metabolism*
  • Plant Extracts / metabolism*
  • Plant Proteins / chemistry*
  • Protein Conformation*
  • Seeds / chemistry*
  • Sequence Homology

Substances

  • Plant Extracts
  • Plant Proteins

Grants and funding

This work was funded by Department of Biotechnology, Ministry of Science and Technology grant .