Structural highlights
Function
A0A371E4L6_MUCPR
Publication Abstract from PubMed
The structure of the MP-4 protein was previously determined at a resolution of 2.8 A. 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 A) 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.
The structure of MP-4 from Mucuna pruriens at 2.22 A resolution.,Jain A, Kumar A, Shikhi M, Kumar A, Nair DT, Salunke DM Acta Crystallogr F Struct Biol Commun. 2020 Feb 1;76(Pt 2):47-57. doi:, 10.1107/S2053230X20000199. Epub 2020 Feb 3. PMID:32039885[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jain A, Kumar A, Shikhi M, Kumar A, Nair DT, Salunke DM. The structure of MP-4 from Mucuna pruriens at 2.22 A resolution. Acta Crystallogr F Struct Biol Commun. 2020 Feb 1;76(Pt 2):47-57. doi:, 10.1107/S2053230X20000199. Epub 2020 Feb 3. PMID:32039885 doi:http://dx.doi.org/10.1107/S2053230X20000199