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One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase.

Abstract：

:Acireductone dioxygenase (ARD) catalyzes different reactions between O2 and 1,2-dihydroxy-3-oxo-5-(methylthio)pent-1-ene (acireductone) depending upon the metal bound in the active site. Ni2+ -ARD cleaves acireductone to formate, CO and methylthiopropionate. If Fe2+ is bound (ARD'), the same substrates yield methylthioketobutyrate and formate. The two forms differ in structure, and are chromatographically separable. Paramagnetism of Fe2+ renders the active site of ARD' inaccessible to standard NMR methods. The structure of ARD' has been determined using Fe2+ binding parameters determined by X-ray absorption spectroscopy and NMR restraints from H98S ARD, a metal-free diamagnetic protein that is isostructural with ARD'. ARD' retains the beta-sandwich fold of ARD, but a structural entropy switch increases order at one end of a two-helix system that bisects the beta-sandwich and decreases order at the other upon interconversion of ARD and ARD', causing loss of the C-terminal helix in ARD' and rearrangements of residues involved in substrate orientation in the active site.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Ju T,Goldsmith RB,Chai SC,Maroney MJ,Pochapsky SS,Pochapsky TC

doi

10.1016/j.jmb.2006.08.060

subject

Has Abstract

pub_date

2006-11-03 00:00:00

pages

823-34

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(06)01113-2

journal_volume

363

pub_type

杂志文章

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