On the Role and Structural Outlook of Carboxy-Terminal Domain of Anabaena Sensory Rhodopsin

Authors: Trivedi VD*, Oscar-Okpala T, Pangira P and Vernier BT

DOI: 10.23880/ijbp-16000247

Volume 9, Issue 1

Abstract

Anabaena Sensory Rhodopsin, ASR represents a small family of sensory rhodopsins among a vast family of microbial rhodopsins. In contrast to other microbial sensory rhodopsins, which are known to mediate photostimulated signal relay using cognate membrane transducer, ASR interacts to plausible soluble oligomeric transducer protein. Though the atomic resolution structure ASR is available, it only included only the transmembrane domain. Interestingly the available structure is remarkably different from other microbial sensory rhodopsins, with presence of water. Additionally, the sequence of missing cytoplasmic domain contains a series of positively charged Arginine residues in it. Authors have outlined the influence of this domain in addition to flexible structural outlook using Deep Mind’s Nova Fold-2. Authors propose that charged amino acids are vital in ASR-transducer interaction. Subsequent attempts to explore the molecular basis of ASR and cognate transducer binding would be vital to understand the unique photo-mediated signal cascade in Anabaena PCC 7120.

Keywords: Microbial Rhodopsins; 7-TM [Transmembrane]; Retinal Chromophore; Anabaena PCC7120; Transducer; Photomediated Signaling

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