Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Single-particle EM reveals the higher-order domain architecture of soluble guanylate cyclase.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 111, Issue 8, Page 2960-2965, Year 2014
Publish date	Feb 25, 2014
Authors	Melody G Campbell / Eric S Underbakke / Clinton S Potter / Bridget Carragher / Michael A Marletta /
PubMed Abstract	Soluble guanylate cyclase (sGC) is the primary nitric oxide (NO) receptor in mammals and a central component of the NO-signaling pathway. The NO-signaling pathways mediate diverse physiological ...Soluble guanylate cyclase (sGC) is the primary nitric oxide (NO) receptor in mammals and a central component of the NO-signaling pathway. The NO-signaling pathways mediate diverse physiological processes, including vasodilation, neurotransmission, and myocardial functions. sGC is a heterodimer assembled from two homologous subunits, each comprised of four domains. Although crystal structures of isolated domains have been reported, no structure is available for full-length sGC. We used single-particle electron microscopy to obtain the structure of the complete sGC heterodimer and determine its higher-order domain architecture. Overall, the protein is formed of two rigid modules: the catalytic dimer and the clustered Per/Art/Sim and heme-NO/O2-binding domains, connected by a parallel coiled coil at two hinge points. The quaternary assembly demonstrates a very high degree of flexibility. We captured hundreds of individual conformational snapshots of free sGC, NO-bound sGC, and guanosine-5'-[(α,β)-methylene]triphosphate-bound sGC. The molecular architecture and pronounced flexibility observed provides a significant step forward in understanding the mechanism of NO signaling.
External links	Proc Natl Acad Sci U S A / PubMed:24516165 / PubMed Central
Methods	EM (single particle)
Resolution	30.0 Å
Structure data	EMDB-5861: Single-particle reconstruction of conformation I of ligand-free sGC (straight) Method: EM (single particle) / Resolution: 30.0 Å EMDB-5862: Single-particle reconstruction of conformation II of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5863: Single-particle reconstruction of conformation III of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5864: Single-particle reconstruction of conformation IV of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5865: Single-particle reconstruction of conformation V of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5866: Single-particle reconstruction of conformation VI of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5867: Single-particle reconstruction of conformation VII of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5868: Single-particle reconstruction of conformation VIII of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5869: Single-particle reconstruction of conformation IX of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5870: Single-particle reconstruction of conformation X of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5871: Single-particle reconstruction of conformation XI of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5872: Single-particle reconstruction of conformation XII of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5873: Single-particle reconstruction of conformation XIII of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5874: Single-particle reconstruction of conformation XIV of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5875: Single-particle reconstruction of conformation XV of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5876: Single-particle reconstruction of conformation XVI of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5877: Single-particle reconstruction of conformation XVII of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5878: Single-particle reconstruction of conformation XVIII of ligand-free sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5879: Single-particle reconstruction of conformation I of NO-bound sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5880: Single-particle reconstruction of conformation II of NO-bound sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5881: Single-particle reconstruction of conformation I of GPCPP-bound sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5882: Single-particle reconstruction of conformation II of GPCPP-bound sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5883: Single-particle reconstruction of conformation I of GPCPP-bound and NO-bound sGC Method: EM (single particle) / Resolution: 30.0 Å EMDB-5884: Single-particle reconstruction of conformation II of GPCPP-bound and NO-bound sGC Method: EM (single particle) / Resolution: 30.0 Å
Source	Rattus norvegicus (Norway rat)