Structural highlights
Function
I6YCP0_MYCTU
Publication Abstract from PubMed
The genome of the human pathogen Mycobacterium tuberculosis (Mtb) encodes approximately 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.
Mycobacterium tuberculosis Rv3651 is a triple sensor-domain protein.,Abendroth J, Frando A, Phan IQ, Staker BL, Myler PJ, Edwards TE, Grundner C Protein Sci. 2018 Feb;27(2):568-572. doi: 10.1002/pro.3343. Epub 2017 Dec 5. PMID:29119630[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Abendroth J, Frando A, Phan IQ, Staker BL, Myler PJ, Edwards TE, Grundner C. Mycobacterium tuberculosis Rv3651 is a triple sensor-domain protein. Protein Sci. 2018 Feb;27(2):568-572. doi: 10.1002/pro.3343. Epub 2017 Dec 5. PMID:29119630 doi:http://dx.doi.org/10.1002/pro.3343