1e65: Difference between revisions
New page: left|200px<br /><applet load="1e65" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e65, resolution 1.85Å" /> '''AZURIN FROM PSEUDOMO... |
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[[Image:1e65.gif|left|200px]]<br /><applet load="1e65" size=" | [[Image:1e65.gif|left|200px]]<br /><applet load="1e65" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1e65, resolution 1.85Å" /> | caption="1e65, resolution 1.85Å" /> | ||
'''AZURIN FROM PSEUDOMONAS AERUGINOSA, APO FORM'''<br /> | '''AZURIN FROM PSEUDOMONAS AERUGINOSA, APO FORM'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1E65 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http:// | 1E65 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: electron transport(copper binding)]] | [[Category: electron transport(copper binding)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:36:44 2008'' | ||
Revision as of 14:36, 23 January 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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