6SIR

Crystal structure of the guanylate cyclase domain of RhGC from Catenaria anguillulae in complex with GTP

Summary for 6SIR

• Entry DOI: 10.2210/pdb6sir/pdb
• Descriptor: Nucleotide cyclase, CALCIUM ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: guanylate cyclase, lyase
• Biological source: Catenaria anguillulae PL171
• Total number of polymer chains: 4
• Total formula weight: 84695.10

Authors

Butryn, A.,Orville, A.M. (deposition date: 2019-08-10, release date: 2019-12-18, Last modification date: 2024-01-24)

Primary citation

Butryn, A.,Raza, H.,Rada, H.,Moraes, I.,Owens, R.J.,Orville, A.M.
Molecular basis for GTP recognition by light-activated guanylate cyclase RhGC.
Febs J., 287:2797-2807, 2020

PubMed Abstract: Cyclic guanosine 3',5'-monophosphate (cGMP) is an intracellular signalling molecule involved in many sensory and developmental processes. Synthesis of cGMP from GTP is catalysed by guanylate cyclase (GC) in a reaction analogous to cAMP formation by adenylate cyclase (AC). Although detailed structural information is available on the catalytic region of nucleotidyl cyclases (NCs) in various states, these atomic models do not provide a sufficient explanation for the substrate selectivity between GC and AC family members. Detailed structural information on the GC domain in its active conformation is largely missing, and no crystal structure of a GTP-bound wild-type GC domain has been published to date. Here, we describe the crystal structure of the catalytic domain of rhodopsin-GC (RhGC) from Catenaria anguillulae in complex with GTP at 1.7 Å resolution. Our study reveals the organization of a eukaryotic GC domain in its active conformation. We observe that the binding mode of the substrate GTP is similar to that of AC-ATP interaction, although surprisingly not all of the interactions predicted to be responsible for base recognition are present. The structure provides insights into potential mechanisms of substrate discrimination and activity regulation that may be common to all class III purine NCs. DATABASE: Structural data are available in Protein Data Bank database under the accession number 6SIR. ENZYMES: EC4.6.1.2.

PubMed: 31808997
DOI: 10.1111/febs.15167

Experimental method

X-RAY DIFFRACTION (1.7 Å)