Mycobacterium tuberculosis Rv3651 is a triple sensor‐domain protein |
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| Authors: | Jan Abendroth Andrew Frando Isabelle Q Phan Bart L Staker Peter J Myler Thomas E Edwards Christoph Grundner |
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| Institution: | 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 |
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| 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 cG 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. |
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| Keywords: | proteins of unknown function PAS domain GAF domain Mycobacterium tuberculosis |
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