3hls

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

spinqualitylabelsall models 3hls, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hls is a 8 chain structure with sequence from Rattus norvegicus. The January 2011 RCSB PDB Molecule of the Month feature on Nitric Oxide Synthase by David Goodsell is 10.2210/rcsb_pdb/mom_2011_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GCYB1_RAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed BACKGROUND: 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. RESULTS: To investigate the structure of the CC S-helix region, we crystallized and determined the structure of the CC domain of the sGCbeta1 subunit comprising residues 348-409. The crystal structure was refined to 2.15 A resolution. CONCLUSIONS: The CC structure of sGCbeta1 revealed a tetrameric arrangement comprised of a dimer of CC dimers. Each monomer is comprised of a long a-helix, a turn near residue P399, and a short second a-helix. The CC structure also offers insights as to how sGC homodimers are not as stable as (functionally) active heterodimers via a possible role for inter-helix salt-bridge formation. The structure also yielded insights into the residues involved in dimerization. In addition, the CC region is also known to harbor a number of congenital and man-made mutations in both membrane and soluble guanylyl cyclases and those function-affecting mutations have been mapped onto the CC structure. This mutant analysis indicated an importance for not only certain dimerization residue positions, but also an important role for other faces of the CC dimer which might perhaps interact with adjacent domains. Our results also extend beyond guanylyl cyclases as the CC structure is, to our knowledge, the first S-helix structure and serves as a model for all S-helix containing family members. Crystal structure of the signaling helix coiled-coil domain of the beta1 subunit of the soluble guanylyl cyclase.,Ma X, Beuve A, van den Akker F BMC Struct Biol. 2010 Jan 27;10:2. PMID:20105301 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Guanylate cyclase 3D structures

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