STAC--A New Domain Associated with Transmembrane Solute Transport and Two-Component Signal Transduction Systems

Journal of Molecular Biology
Mateusz KorycinskiAndrei N Lupas

Abstract

Transmembrane receptors are integral components of sensory pathways in prokaryotes. These receptors share a common dimeric architecture, consisting in its basic form of an N-terminal extracellular sensor, transmembrane helices, and an intracellular effector. As an exception, we have identified an archaeal receptor family--exemplified by Af1503 from Archaeoglobus fulgidus--that is C-terminally shortened, lacking a recognizable effector module. Instead, a HAMP domain forms the sole extension for signal transduction in the cytosol. Here, we examine the gene environment of Af1503-like receptors and find a frequent association with transmembrane transport proteins. Furthermore, we identify and define a closely associated new protein domain family, which we characterize structurally using Af1502 from A. fulgidus. Members of this family are found both as stand-alone proteins and as domains within extant receptors. In general, the latter appear as connectors between the solute carrier 5 (SLC5)-like transmembrane domains and two-component signal transduction (TCST) domains. This is seen, for example, in the histidine kinase CbrA, which is a global regulator of metabolism, virulence, and antibiotic resistance in Pseudomonads. We propose ...Continue Reading

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Citations

Aug 16, 2016·Journal of Molecular Biology·Christopher P ZschiedrichHendrik Szurmant
Oct 17, 2015·Proteins·Andriy KryshtafovychTorsten Schwede
Sep 19, 2018·Journal of Bacteriology·Itai MuzhingiAlexandra E Purdy
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Dec 28, 2017·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Ivan Gushchin, Valentin Gordeliy
Mar 28, 2020·Scientific Reports·Larissa WirtzHeinrich Jung
Mar 7, 2021·International Journal of Molecular Sciences·Tania HenriquezHeinrich Jung
Aug 28, 2021·Proteins·Andriy KryshtafovychUNKNOWN AlphaFold2 team

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