Nature Search

Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex

The allosteric regulation of the bienzyme complex imidazole glycerol phosphate synthase (HisFH) remains to be elucidated. Here, the authors provide structural insights into the dynamic allosteric mechanism by which ligand binding to the cyclase and glutaminase active sites of HisFH regulate enzyme activation.

Jan Philip Wurm
Sihyun Sung
Remco Sprangers
ResearchOpen Access12 May 2021
Nature Communications

Volume: 12, P: 1-13
Observation of conformational changes that underlie the catalytic cycle of Xrn2

Using methyl group and fluorine NMR spectroscopic methods, Overbeck et al revealed that the dynamics of the eukaryotic 5′→3′ exoribonuclease Xrn2 in the region around the active site are correlated with its catalytic activity.

Jan H. Overbeck
David Stelzig
Remco Sprangers
ResearchOpen Access25 Aug 2022
Nature Chemical Biology

Volume: 18, P: 1152-1160
The Rrp4–exosome complex recruits and channels substrate RNA by a unique mechanism

A methyl-TROSY NMR approach provides a detailed model for how the archaeal exosome cap recruits multiple RNA substrates and channels them one by one into the catalytic barrel for degradation.

Milos A Cvetkovic
Jan Philip Wurm
Remco Sprangers
Research13 Mar 2017
Nature Chemical Biology

Volume: 13, P: 522-528
Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS

Rhabdopeptides are synthesized by non-ribosomal peptide synthetases (NRPSs) and the multiple NRPS subunits interact through docking domains (DD). Here the authors provide insights into DD interaction patterns and present the structures of three N-terminal docking domains (^NDD) and a ^NDD-^CDD complex and derive a set of recognition rules for DD interactions.

Carolin Hacker
Xiaofeng Cai
Jens Wöhnert
ResearchOpen Access19 Oct 2018
Nature Communications

Volume: 9, P: 1-11

Quick links

Search

Filter By:

Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex

Observation of conformational changes that underlie the catalytic cycle of Xrn2

The Rrp4–exosome complex recruits and channels substrate RNA by a unique mechanism

Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS

Search

Quick links