…
comment: The repository administrator has not yet configured an RDF license.
primary topic: Global shape of SvGT, a metal-dependent bacteriocin modifying S/O-HexNActransferase from actinobacteria: c -terminal dimerization modulates the function of this GT

Global shape of SvGT, a metal-dependent bacteriocin modifying S/O-HexNActransferase from actinobacteria: c -terminal dimerization modulates the function of this GT
type: AcademicArticle
type: Article
abstract: Here, we describe hitherto unknown shape-function of S/O-HexNActransferase SvGT (ORF AQF52_3101) instrumental in glycosylation of bacteriocin SvC (ORF AQF52_3099) in Streptomyces venezuelae ATCC 15439. Data from gel filtration, mass spectrometry, analytical ultracentrifugation, and Small Angle X-ray Scattering (SAXS), experiments confirmed elongated dimeric shape in solution for SvGT protein. Enzyme assays confirmed the dependence of SvGT on the availability of Mg2+ ions to be functionally activated. SAXS data analysis provided that apo and Mg2+-activated protein adopt a shape characterized by a radius of gyration and maximum linear dimension of 5.2 and 17.0 nm, and 5.3 and 17.8 nm, respectively. Alphafold2 server was used to model the monomeric chain of this protein which was docked on self to obtain different poses of the dimeric entity. Experimental SAXS data was used to select and refine the structure of SvGT dimer. Results showed that Mg2+ ions induce reorientation of the GT domain of one chain leading to a dimer with C2 symmetry, and the C-terminal portion entangles with each other in all states. Mutation-rendered alteration in activity profiles confirmed the role of conserved residues around catalytic motif. Global structure analysis puts forth the need to understand the role of constitutionally diverse C-terminal portion in regulating substrate selectivity.Communicated by Ramaswamy H. Sarma.
date: 2023-09-15
volume: 42
issue: 19
status: peerReviewed
status: published
author list: authors
type: EPrint
type: ArticleEPrint
is part of: repository
subject: QR Microbiology

J. Biomol. Struct. Dyn.
type: Collection

Alka Rao
type: Person
given name: Alka
family name: Rao

Yogita Sharma
type: Person
given name: Yogita
family name: Sharma

Ashish Ashish
type: Person
given name: Ashish
family name: Ashish

Shimona Ahlawat
type: Person
given name: Shimona
family name: Ahlawat

HTML Summary of #3393 Global shape of SvGT, a metal-dependent bacteriocin modifying S/O-HexNActransferase from actinobacteria: c -terminal dimerization modulates the function of this GT
format: text/html
primary topic: Global shape of SvGT, a metal-dependent bacteriocin modifying S/O-HexNActransferase from actinobacteria: c -terminal dimerization modulates the function of this GT

QR Microbiology
type: Concept