3lai | pdb_00003lai

Structural insights into the molecular mechanism of H-NOX activation

spinqualitylabelsall models 3lai, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3lai is a 3 chain structure with sequence from Caldanaerobacter subterraneus subsp. tengcongensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.144Å Ligands: HEM, IMD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8RBX6_CALS4 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 Nitric oxide (NO) signaling in mammals controls important processes such as smooth muscle relaxation and neurotransmission by activation of soluble guanylate cyclase (sGC). NO binding to the heme domain of sGC leads to dissociation of the iron-histidine (Fe-His) bond, which is required for enzyme activity. The heme domain of sGC belongs to a larger class of proteins called H-NOX (Heme Nitric oxide/OXygen) domains. Previous crystallographic studies on H-NOX domains demonstrate a correlation between heme bending and protein conformation. It was unclear, however, whether these structural changes were important for signal transduction. Subsequent NMR solution structures of H-NOX proteins show a conformational change, upon disconnection of the heme and proximal helix, similar to those observed in the crystallographic studies. The atomic details of these conformational changes, however, are lacking in the NMR structures especially at the heme pocket. Here, a high-resolution crystal structure of an H-NOX mutant mimicking a broken Fe-His bond is reported. This mutant exhibits specific changes in heme conformation and major N-terminal displacements relative to the wild-type H-NOX protein. Fe-His ligation is ubiquitous in all H-NOX domains, and therefore, the heme and protein conformational changes observed in the present study are likely to occur throughout the H-NOX family when NO binding leads to rupture of the Fe-His bond. Structural insights into the molecular mechanism of H-NOX activation.,Olea C Jr, Herzik MA Jr, Kuriyan J, Marletta MA Protein Sci. 2010 Feb 16. PMID:20162612 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chemotaxis protein 3D structures Methyl-accepting chemotaxis protein

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