5OYH

crystal structure of the catalytic core of a rhodopsin-guanylyl cyclase with converted specificity in complex with ATPalphaS

Summary for 5OYH

• Entry DOI: 10.2210/pdb5oyh/pdb
• Descriptor: Nucleotide cyclase, ADENOSINE-5'-SP-ALPHA-THIO-TRIPHOSPHATE, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: nucleotide cyclase, inhibitor, lyase
• Biological source: Catenaria anguillulae PL171
• Total number of polymer chains: 16
• Total formula weight: 355251.99

Authors

Broser, M.,Scheib, U.,Hegemann, P. (deposition date: 2017-09-09, release date: 2018-06-06, Last modification date: 2024-05-08)

Primary citation

Scheib, U.,Broser, M.,Constantin, O.M.,Yang, S.,Gao, S.,Mukherjee, S.,Stehfest, K.,Nagel, G.,Gee, C.E.,Hegemann, P.
Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 angstrom structure of the adenylyl cyclase domain.
Nat Commun, 9:2046-2046, 2018

PubMed Abstract: The cyclic nucleotides cAMP and cGMP are important second messengers that orchestrate fundamental cellular responses. Here, we present the characterization of the rhodopsin-guanylyl cyclase from Catenaria anguillulae (CaRhGC), which produces cGMP in response to green light with a light to dark activity ratio >1000. After light excitation the putative signaling state forms with τ = 31 ms and decays with τ = 570 ms. Mutations (up to 6) within the nucleotide binding site generate rhodopsin-adenylyl cyclases (CaRhACs) of which the double mutated YFP-CaRhAC (E497K/C566D) is the most suitable for rapid cAMP production in neurons. Furthermore, the crystal structure of the ligand-bound AC domain (2.25 Å) reveals detailed information about the nucleotide binding mode within this recently discovered class of enzyme rhodopsin. Both YFP-CaRhGC and YFP-CaRhAC are favorable optogenetic tools for non-invasive, cell-selective, and spatio-temporally precise modulation of cAMP/cGMP with light.

PubMed: 29799525
DOI: 10.1038/s41467-018-04428-w

Experimental method

X-RAY DIFFRACTION (2.249 Å)