3nvu | pdb_00003nvu

Modulating Heme Redox Potential Through Protein-Induced Porphyrin Distortion

spinqualitylabelsall models 3nvu, resolution 2.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3nvu is a 2 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. Ligands: CL, HEM, OXY Related: 1u55, 3nvr Gene: Tar4, TTE0680 (Caldanaerobacter subterraneus subsp. tengcongensis) Resources: FirstGlance, OCA, RCSB, PDBsum 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 Hemoproteins are ubiquitous in biology and are commonly involved in critical processes such as electron transfer, oxidative phosphorylation, and signal transduction. Both the protein environment and the heme cofactor contribute to generate the range of chemical properties needed for these diverse functions. Using the heme nitric oxide/oxygen binding (H-NOX) protein from the thermophilic bacterium Thermoanaerobacter tengcongensis, we have shown that heme electronic properties can be modulated by porphyrin distortion within the same protein scaffold without changing the heme ligation state or heme environment. The degree of heme distortion was found to be directly correlated to the electron density at the heme iron, as evidenced by dramatic changes in the heme redox potential and pK(a) of the distal ligand ((-)OH vs H(2)O). Protein-induced porphyrin distortion represents a new strategy to rationally tune the electronic properties of protein-bound porphyrins and could be used to engineer proteins with desired reactivity or functionality. Modulating Heme Redox Potential through Protein-Induced Porphyrin Distortion.,Olea C, Kuriyan J, Marletta MA J Am Chem Soc. 2010 Aug 25. PMID:20735135 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chemotaxis protein Methyl-accepting chemotaxis protein

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