3jt2 | pdb_00003jt2

Cu(II) N47S/M121L variant of Pseudomonas Aeruginosa azurin

spinqualitylabelsall models 3jt2, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3jt2 is a 2 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU Related: 3jtb Gene: azu, Azurin, PA4922 ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase. 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 Redox processes are at the heart of numerous functions in chemistry and biology, from long-range electron transfer in photosynthesis and respiration to catalysis in industrial and fuel cell research. These functions are accomplished in nature by only a limited number of redox-active agents. A long-standing issue in these fields is how redox potentials are fine-tuned over a broad range with little change to the redox-active site or electron-transfer properties. Resolving this issue will not only advance our fundamental understanding of the roles of long-range, non-covalent interactions in redox processes, but also allow for design of redox-active proteins having tailor-made redox potentials for applications such as artificial photosynthetic centres or fuel cell catalysts for energy conversion. Here we show that two important secondary coordination sphere interactions, hydrophobicity and hydrogen-bonding, are capable of tuning the reduction potential of the cupredoxin azurin over a 700 mV range, surpassing the highest and lowest reduction potentials reported for any mononuclear cupredoxin, without perturbing the metal binding site beyond what is typical for the cupredoxin family of proteins. We also demonstrate that the effects of individual structural features are additive and that redox potential tuning of azurin is now predictable across the full range of cupredoxin potentials. Rationally tuning the reduction potential of a single cupredoxin beyond the natural range.,Marshall NM, Garner DK, Wilson TD, Gao YG, Robinson H, Nilges MJ, Lu Y Nature. 2009 Nov 5;462(7269):113-6. PMID:19890331 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Azurin

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