3et6

The crystal structure of the catalytic domain of a eukaryotic guanylate cyclaseThe crystal structure of the catalytic domain of a eukaryotic guanylate cyclase

Structural highlights 3et6 is a 2 chain structure with sequence from Chlamydomonas reinhardtii. 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 2.55Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5YLC2_CHLRE 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: Soluble guanylate cyclases generate cyclic GMP when bound to nitric oxide, thereby linking nitric oxide levels to the control of processes such as vascular homeostasis and neurotransmission. The guanylate cyclase catalytic module, for which no structure has been determined at present, is a class III nucleotide cyclase domain that is also found in mammalian membrane-bound guanylate and adenylate cyclases. RESULTS: We have determined the crystal structure of the catalytic domain of a soluble guanylate cyclase from the green algae Chlamydomonas reinhardtii at 2.55 A resolution, and show that it is a dimeric molecule. CONCLUSION: Comparison of the structure of the guanylate cyclase domain with the known structures of adenylate cyclases confirms the close similarity in architecture between these two enzymes, as expected from their sequence similarity. The comparison also suggests that the crystallized guanylate cyclase is in an inactive conformation, and the structure provides indications as to how activation might occur. We demonstrate that the two active sites in the dimer exhibit positive cooperativity, with a Hill coefficient of approximately 1.5. Positive cooperativity has also been observed in the homodimeric mammalian membrane-bound guanylate cyclases. The structure described here provides a reliable model for functional analysis of mammalian guanylate cyclases, which are closely related in sequence. The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase.,Winger JA, Derbyshire ER, Lamers MH, Marletta MA, Kuriyan J BMC Struct Biol. 2008 Oct 7;8:42. PMID:18842118 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Guanylate cyclase 3D structures

spinqualitylabelsall models 3et6, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image