4fdk

F78L Tt H-NOX

spinqualitylabelsall models 4fdk, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fdk is a 2 chain structure with sequence from Caldanaerobacter subterraneus subsp. tengcongensis MB4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: HEM, OXY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8RBX6_CALS4 Publication Abstract from PubMed The role of pi-stacking in controlling redox and ligand binding properties of porphyrins has been of interest for many years. The recent discovery of H-NOX domains has provided a model system to investigate the role of porphyrin pi-stacking within a heme protein scaffold. Removal of a phenylalanine-porphyrin pi-stack dramatically increased O2, NO, and CO affinities and caused changes in redox potential (~40mV) without any structural changes. These results suggest that small changes in redox potential affect ligand affinity and that pi-stacking may provide a novel route to engineer heme protein properties for new functions. Porphyrin pi-stacking in a heme protein scaffold tunes gas ligand affinity.,Weinert EE, Phillips-Piro CM, Marletta MA J Inorg Biochem. 2013 Jun 15;127C:7-12. doi: 10.1016/j.jinorgbio.2013.06.004. PMID:23831583 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chemotaxis protein 3D structures

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