1e65

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1e65, resolution 1.85Å

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AZURIN FROM PSEUDOMONAS AERUGINOSA, APO FORM

Overview

The 3D structure of apo-azurin from Pseudomonas aeruginosa has been, determined at 1.85 A resolution. The crystal structure is composed of two, different molecular forms of apo-azurin arranged as hetero-dimers in the, tetramer of the asymmetric unit. Form 1 closely resembles the holo-protein, lacking copper. Form 2 shows differences in the metal binding site region, induced by the incorporation of a solvent molecule into this site. The, positions of the copper ligands His46 and His117 are shifted by 0.6 A and, 1.6 A. The His117 side chain adopts a position at the surface of the, protein, thereby facilitating access to the copper site. The presence of, two different molecular forms of apo-azurin in the crystal lattice may, reflect an equilibrium between the two forms in solution. 1H-NMR spectra, of apo-azurin recorded as a function of pH show that at high pH the line, broadening of His35, His46 and His117 resonances is consistent with an, interconversion between forms 1 and 2. At low pH, no broadening is, observed. This may indicate that here the interconversion is fast on the, NMR timescale.

About this Structure

1E65 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 A resolution., Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW, FEBS Lett. 1992 Jul 20;306(2-3):119-24. PMID:1633865

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