3NP3

C112D/M121E Pseudomonas Aeruginosa Azurin

Summary for 3NP3

• Entry DOI: 10.2210/pdb3np3/pdb
• Related: 3NP4 3OQR
• Descriptor: Azurin, COPPER (II) ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: cupredoxin, azurin, electron transport
• Biological source: Pseudomonas aeruginosa
• Cellular location: Periplasm: P00282
• Total number of polymer chains: 1
• Total formula weight: 14220.90

Authors

Lancaster, K.M.,Gray, H.B. (deposition date: 2010-06-27, release date: 2010-10-13, Last modification date: 2024-11-20)

Primary citation

Lancaster, K.M.,Sproules, S.,Palmer, J.H.,Richards, J.H.,Gray, H.B.
Outer-Sphere Effects on Reduction Potentials of Copper Sites in Proteins: The Curious Case of High Potential Type 2 C112D/M121E Pseudomonas aeruginosa Azurin.
J.Am.Chem.Soc., 132:14590-14595, 2010

PubMed Abstract: 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 (∼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.

PubMed: 20879734
DOI: 10.1021/ja105731x

Experimental method

X-RAY DIFFRACTION (2.1 Å)