1e65: Difference between revisions
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[[Image:1e65.gif|left|200px]] | [[Image:1e65.gif|left|200px]] | ||
'''AZURIN FROM PSEUDOMONAS AERUGINOSA, APO FORM''' | {{Structure | ||
|PDB= 1e65 |SIZE=350|CAPTION= <scene name='initialview01'>1e65</scene>, resolution 1.85Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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}} | |||
'''AZURIN FROM PSEUDOMONAS AERUGINOSA, APO FORM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E65 is a [ | 1E65 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E65 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1633865 1633865] | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: electron transport(copper binding)]] | [[Category: electron transport(copper binding)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:50:22 2008'' | ||
Revision as of 11:50, 20 March 2008
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AZURIN FROM PSEUDOMONAS AERUGINOSA, APO FORM
OverviewOverview
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 StructureAbout this Structure
1E65 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
ReferenceReference
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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