Abstract:
:Processive chitinase is a linear molecular motor which moves on the surface of crystalline chitin driven by processive hydrolysis of single chitin chain. Here, we analyse the mechanism underlying unidirectional movement of Serratia marcescens chitinase A (SmChiA) using high-precision single-molecule imaging, X-ray crystallography, and all-atom molecular dynamics simulation. SmChiA shows fast unidirectional movement of ~50 nm s-1 with 1 nm forward and backward steps, consistent with the length of reaction product chitobiose. Analysis of the kinetic isotope effect reveals fast substrate-assisted catalysis with time constant of ~3 ms. Decrystallization of the single chitin chain from crystal surface is the rate-limiting step of movement with time constant of ~17 ms, achieved by binding free energy at the product-binding site of SmChiA. Our results demonstrate that SmChiA operates as a burnt-bridge Brownian ratchet wherein the Brownian motion along the single chitin chain is rectified forward by substrate-assisted catalysis.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Nakamura A,Okazaki KI,Furuta T,Sakurai M,Iino Rdoi
10.1038/s41467-018-06362-3subject
Has Abstractpub_date
2018-09-19 00:00:00pages
3814issue
1issn
2041-1723pii
10.1038/s41467-018-06362-3journal_volume
9pub_type
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