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Protein Sci. 2018 Feb;27(2):568-572. doi: 10.1002/pro.3343. Epub 2017 Dec 5.

Mycobacterium tuberculosis Rv3651 is a triple sensor-domain protein.

Author information

1
Beryllium Discovery, Bainbridge Island, Washington.
2
Seattle Structural Genomics Center for Infectious Disease, Seattle, Washington.
3
Center for Infectious Disease Research (formerly Seattle Biomedical Research Institute), Seattle, Washington.
4
Department of Global Health, University of Washington, Seattle, Washington.
5
Department of Biomedical Informatics and Medical Education, University of Washington, Seattle, Washington.

Abstract

The genome of the human pathogen Mycobacterium tuberculosis (Mtb) encodes ∼4,400 proteins, but one third of them have unknown functions. We solved the crystal structure of Rv3651, a hypothetical protein with no discernible similarity to proteins with known function. Rv3651 has a three-domain architecture that combines one cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA (GAF) domain and two Per-ARNT-Sim (PAS) domains. GAF and PAS domains are sensor domains that are typically linked to signaling effector molecules. Unlike these sensor-effector proteins, Rv3651 is an unusual sensor domain-only protein with highly divergent sequence. The structure suggests that Rv3651 integrates multiple different signals and serves as a scaffold to facilitate signal transfer.

KEYWORDS:

GAF domain; Mycobacterium tuberculosis; PAS domain; proteins of unknown function

PMID:
29119630
PMCID:
PMC5775179
[Available on 2019-02-01]
DOI:
10.1002/pro.3343

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