Catalysis by a rigid enzyme
Ben Bdira, F.; Waudby, C. A.; N. Volkov, A.; Schroder, S.; AB, E.; Codee, J.; Overkleeft, H. S.; Aerts, H.; van Ingen, H.; Ubbink, M.
Show abstract
Many enzymes are dynamic entities, sampling conformational states that are relevant for catalytic activity. Crystal structures of catalytic intermediates suggest, however, that not all enzymes require structural changes for activity. The single-domain enzyme xylanase from Bacillus circulans (BCX) is involved in the degradation of hemicellulose. We demonstrate that BCX in solution undergoes minimal structural changes during catalysis. NMR spectroscopy results show that the rigid protein matrix provides a frame for fast substrate binding in multiple conformations, accompanied by slow, enzyme induced substrate distortion. Therefore, we propose a model in which the rigid enzyme takes advantage of substrate flexibility to induce a conformation that facilitates catalysis.\n\nOne Sentence SummaryThe rigid matrix of BCX uses substrate flexibility in Michaelis complex formation.
Matching journals
The top 6 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate 96%
- Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA 94%
- Unexpected Specificity within Dynamic Transcriptional Protein-Protein Complexes 94%
Similar papers in this journal
- Ligand Entry into Fatty Acid Binding Protein via Local Unfolding instead of Gap Widening 95%
- Structural basis for the hyperthermostability of an archaeal glutaminase induced by post-translational succinimide formation 95%
- NMR reveals light-induced changes in the dynamics of a photoswitchable fluorescent protein 95%
Similar papers in this journal
- The nucleotide exchange factor, GrpE, modulates substrate affinity by interaction of its N-terminal tails with the DnaK substrate-binding domain. 94%
- Identification of Small Molecule Ligand Binding Sites On and In the ARNT PAS-B Domain 94%
- The structure of the SufS-SufE complex reveals interactions driving protected persulfide transfer in iron-sulfur cluster biogenesis 94%
Similar papers in this journal
- Light-dependent flavin redox and adduct states control the conformation and DNA binding activity of the transcription factor EL222 95%
- Dynamics of the HD regulatory subdomain of PARP 1; substrate access and allostery in PARP activation and inhibition. 95%
- Novel anti-repression mechanism of H-NS proteins by a phage "early protein". 93%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.