Secondary structure reshuffling modulates glycosyltransferase function at the membrane.

Abstract:

:Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant states. The crystal structures of mannosyltransferase PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including β-strand-to-α-helix and α-helix-to-β-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane.

journal_name

Nat Chem Biol

journal_title

Nature chemical biology

authors

Giganti D,Albesa-Jové D,Urresti S,Rodrigo-Unzueta A,Martínez MA,Comino N,Barilone N,Bellinzoni M,Chenal A,Guerin ME,Alzari PM

doi

10.1038/nchembio.1694

subject

Has Abstract

pub_date

2015-01-01 00:00:00

pages

16-8

issue

1

eissn

1552-4450

issn

1552-4469

pii

nchembio.1694

journal_volume

11

pub_type

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