3HLS

Crystal structure of the signaling helix coiled-coil doimain of the BETA-1 subunit of the soluble guanylyl cyclase

Summary for 3HLS

• Entry DOI: 10.2210/pdb3hls/pdb
• Descriptor: Guanylate cyclase soluble subunit beta-1 (2 entities in total)
• Functional Keywords: coiled-coil domain, signaling helix, s-helix, cgmp biosynthesis, cytoplasm, gtp-binding, heme, iron, lyase, metal-binding, nucleotide-binding, signaling protein
• Biological source: Rattus norvegicus (rat)
• Cellular location: Cytoplasm: P20595
• Total number of polymer chains: 8
• Total formula weight: 62549.22

Authors

Ma, X.,van den Akker, F. (deposition date: 2009-05-28, release date: 2010-01-19, Last modification date: 2024-11-27)

Primary citation

Ma, X.,Beuve, A.,van den Akker, F.
Crystal structure of the signaling helix coiled-coil domain of the beta-1 subunit of the soluble guanylyl cyclase.
Bmc Struct.Biol., 10:2-2, 2010

PubMed Abstract: The soluble guanylyl cyclase (sGC) is a heterodimeric enzyme that, upon activation by nitric oxide, stimulates the production of the second messenger cGMP. Each sGC subunit harbor four domains three of which are used for heterodimerization: H-NOXA/H-NOBA domain, coiled-coil domain (CC), and catalytic guanylyl cyclase domain. The CC domain has previously been postulated to be part of a larger CC family termed the signaling helix (S-helix) family. Homodimers of sGC have also been observed but are not functionally active yet are likely transient awaiting their intended heterodimeric partner.

PubMed: 20105301
DOI: 10.1186/1472-6807-10-2

Experimental method

X-RAY DIFFRACTION (2.15 Å)