1e65

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e65 OCA], [http://www.ebi.ac.uk/pdbsum/1e65 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e65 RCSB]</span>
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[[Category: electron transport(copper binding)]]
[[Category: electron transport(copper binding)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:55:58 2008''

Revision as of 16:56, 30 March 2008


PDB ID 1e65

Drag the structure with the mouse to rotate
, resolution 1.85Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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