1pmy
From Proteopedia
(New page: 200px<br /><applet load="1pmy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pmy, resolution 1.5Å" /> '''REFINED CRYSTAL STRUC...) |
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| - | [[Image:1pmy.gif|left|200px]]<br /><applet load="1pmy" size=" | + | [[Image:1pmy.gif|left|200px]]<br /><applet load="1pmy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pmy, resolution 1.5Å" /> | caption="1pmy, resolution 1.5Å" /> | ||
'''REFINED CRYSTAL STRUCTURE OF PSEUDOAZURIN FROM METHYLOBACTERIUM EXTORQUENS AM1 AT 1.5 ANGSTROMS RESOLUTION'''<br /> | '''REFINED CRYSTAL STRUCTURE OF PSEUDOAZURIN FROM METHYLOBACTERIUM EXTORQUENS AM1 AT 1.5 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of pseudoazurin from Methylobacterium extorquens AM1 | + | The crystal structure of pseudoazurin from Methylobacterium extorquens AM1 (PAZAM1) has been solved by the molecular replacement method using copper-copper distances as translation parameters, which were obtained from difference Patterson maps calculated with the synchrotron radiation data containing the multiwavelength anomalous-dispersion effect. The structure refinement was carried out by the use of molecular dynamics optimization and the restrained least-squares method. The final crystallographic R factor was 19.9% for the 14 365 reflections greater than 3sigma between 1.5 and 8.0 A resolution. This report describes the characteristic features of the structure of PAZAM 1 as well as the effectiveness of synchrotron radiation for structure analysis of metalloproteins. The environment of the metal active site and the structural differences among blue-copper proteins are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1PMY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methylobacterium_extorquens Methylobacterium extorquens] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1PMY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methylobacterium_extorquens Methylobacterium extorquens] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: electron transfer(cuproprotein)]] | [[Category: electron transfer(cuproprotein)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:26 2008'' |
Revision as of 12:30, 21 February 2008
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REFINED CRYSTAL STRUCTURE OF PSEUDOAZURIN FROM METHYLOBACTERIUM EXTORQUENS AM1 AT 1.5 ANGSTROMS RESOLUTION
Overview
The crystal structure of pseudoazurin from Methylobacterium extorquens AM1 (PAZAM1) has been solved by the molecular replacement method using copper-copper distances as translation parameters, which were obtained from difference Patterson maps calculated with the synchrotron radiation data containing the multiwavelength anomalous-dispersion effect. The structure refinement was carried out by the use of molecular dynamics optimization and the restrained least-squares method. The final crystallographic R factor was 19.9% for the 14 365 reflections greater than 3sigma between 1.5 and 8.0 A resolution. This report describes the characteristic features of the structure of PAZAM 1 as well as the effectiveness of synchrotron radiation for structure analysis of metalloproteins. The environment of the metal active site and the structural differences among blue-copper proteins are discussed.
About this Structure
1PMY is a Single protein structure of sequence from Methylobacterium extorquens with as ligand. Full crystallographic information is available from OCA.
Reference
Refined crystal structure of pseudoazurin from Methylobacterium extorquens AM1 at 1.5 A resolution., Inoue T, Kai Y, Harada S, Kasai N, Ohshiro Y, Suzuki S, Kohzuma T, Tobari J, Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):317-28. PMID:15299445
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