High-resolution NMR Structure of a Zn2+-containing Form of the Bacteriophage T5 L-alanyl-D-glutamate Peptidase
Document Type
Article
Publication Date
2015
Digital Object Identifier (DOI)
https://doi.org/10.1039/C5RA05993C
Abstract
This paper represents the spatial solution structure of the Zn2+-containing form of the bacteriophage T5 L-alanyl-D-glutamate peptidase (EndoT5-Zn2+). The core of this α + β protein is formed by three α-helices (residues 7–15, 20–30, and 87–104) and a β-sheet containing three β-strands (residues 35–39, 71–76, and 133–135). The protein has two short loops (residues 16–19 and 31–34), a medium-length loop (residues 77–86) containing a short β-hairpin (residues 77–82), and two long loops (residues 40–70 and 105–132). The long loops include a stable 310-helix (residues 66–68) and labile α-helices 46–53 and 113–117. Catalytic Zn2+-binding site is represented by three amino acid residues, His66, Asp73, and His133. The cation-binding His residues are located near the foundations of the long loops, whereas Asp73 is positioned in the middle of the core β-sheet. The catalytic center localization contributes to the stabilization of the entire molecule, with Zn2+-binding playing a key role in the folding of this protein.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
RSC Advances, v. 5, issue 51, p. 41041-41049
Scholar Commons Citation
Prokhorov, Dmitry A.; Mikoulinskaia, Galina V.; Molochkov, Nikolai V.; Uversky, Vladimir N.; and Kutyshenko, Victor P., "High-resolution NMR Structure of a Zn2+-containing Form of the Bacteriophage T5 L-alanyl-D-glutamate Peptidase" (2015). Molecular Medicine Faculty Publications. 390.
https://digitalcommons.usf.edu/mme_facpub/390
