3np3 | pdb_00003np3

C112D/M121E Pseudomonas Aeruginosa Azurin

spinqualitylabelsall models 3np3, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3np3 is a 1 chain structure with sequence from Pseudomonas aeruginosa. 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: CU, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome oxidase. Publication Abstract from PubMed Redox and spectroscopic (electronic absorption, multifrequency electron paramagnetic resonance (EPR), and X-ray absorption) properties together with X-ray crystal structures are reported for the type 2 Cu(II) C112D/M121E variant of Pseudomonas aeruginosa azurin. The results suggest that Cu(II) is constrained from interaction with the proximal glutamate; this structural frustration implies a "rack" mechanism for the 290 mV (vs NHE) reduction potential measured at neutral pH. At high pH ( approximately 9), hydrogen bonding in the outer coordination sphere is perturbed to allow axial glutamate ligation to Cu(II), with a decrease in potential to 119 mV. These results highlight the role played by outer-sphere interactions, and the structural constraints they impose, in determining the redox behavior of transition metal protein cofactors. Outer-Sphere Effects on Reduction Potentials of Copper Sites in Proteins: The Curious Case of High Potential Type 2 C112D/M121E Pseudomonas aeruginosa Azurin.,Lancaster KM, Sproules S, Palmer JH, Richards JH, Gray HB J Am Chem Soc. 2010 Sep 29. PMID:20879734 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Azurin 3D structures

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