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Mycobacterium tuberculosis Rv3651 is a triple sensor‐domain protein
Author(s) -
Abendroth Jan,
Frando Andrew,
Phan Isabelle Q.,
Staker Bart L.,
Myler Peter J.,
Edwards Thomas E.,
Grundner Christoph
Publication year - 2018
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3343
Subject(s) - effector , adenylyl cyclase , mycobacterium tuberculosis , biology , computational biology , protein domain , protein structure , domain (mathematical analysis) , function (biology) , pas domain , hypothetical protein , genetics , microbiology and biotechnology , biochemistry , signal transduction , tuberculosis , gene , transcription factor , mathematical analysis , medicine , mathematics , pathology
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 c G MP‐specific phosphodiesterases, a denylyl cyclases and F hlA (GAF) domain and two P er‐ A RNT‐ S im (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.