Double autoinhibition mechanism of signal transduction ATPases with numerous domains (STAND) with a tetratricopeptide repeat sensor

Nucleic Acids Research
María-Natalia LisaOlivier Danot

Abstract

Upon triggering by their inducer, signal transduction ATPases with numerous domains (STANDs), initially in monomeric resting forms, multimerize into large hubs that activate target macromolecules. This process requires conversion of the STAND conserved core (the NOD) from a closed form encasing an ADP molecule to an ATP-bound open form prone to multimerize. In the absence of inducer, autoinhibitory interactions maintain the NOD closed. In particular, in resting STAND proteins with an LRR- or WD40-type sensor domain, the latter establishes interactions with the NOD that are disrupted in the multimerization-competent forms. Here, we solved the first crystal structure of a STAND with a tetratricopeptide repeat sensor domain, PH0952 from Pyrococcus horikoshii, revealing analogous NOD-sensor contacts. We use this structural information to experimentally demonstrate that similar interactions also exist in a PH0952 homolog, the MalT STAND archetype, and actually contribute to the MalT autoinhibition in vitro and in vivo. We propose that STAND activation occurs by stepwise release of autoinhibitory contacts coupled to the unmasking of inducer-binding determinants. The MalT example suggests that STAND weak autoinhibitory interactions co...Continue Reading

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Citations

Dec 11, 2019·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Patrick WeberAhmed Haouz
Oct 24, 2020·Current Genomics·Avinash Marwal, Rajarshi Kumar Gaur

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Methods Mentioned

BETA
size-exclusion chromatography
X-ray
cross-linking assay
PCR
electrophoresis
nucleotide exchange

Software Mentioned

SHELXD
BLASTP
Aimless
Molprobity
Modeller
HHpred
Phaser
CCP4
MAFFT
Xtriage

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