1qpa
From Proteopedia
(New page: 200px<br /> <applet load="1qpa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qpa, resolution 1.80Å" /> '''LIGNIN PEROXIDASE I...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1QPA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]] with NAG, MAN, CA and HEM as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QPA OCA]]. | + | 1QPA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Basidiomycete_phanerochaete_chrysosporium Basidiomycete phanerochaete chrysosporium]] with NAG, MAN, CA and HEM as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: HE3. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QPA OCA]]. |
==Reference== | ==Reference== | ||
The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle., Choinowski T, Blodig W, Winterhalter KH, Piontek K, J Mol Biol. 1999 Feb 26;286(3):809-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10024453 10024453] | The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle., Choinowski T, Blodig W, Winterhalter KH, Piontek K, J Mol Biol. 1999 Feb 26;286(3):809-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10024453 10024453] | ||
| + | [[Category: Basidiomycete phanerochaete chrysosporium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Choinowski, T.H.]] | [[Category: Choinowski, T.H.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:57:15 2007'' |
Revision as of 08:52, 30 October 2007
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LIGNIN PEROXIDASE ISOZYME LIP4.65 (PI 4.65)
Overview
The crystal structure of lignin peroxidase (LiP) from the white rot fungus, Phanerochaete chrysosporium was refined to an R-factor of 16.2 % utilizing, synchrotron data in the resolution range from 10 to 1.7 A. The final model, comprises all 343 amino acid residues, 370 water molecules, the heme, four, carbohydrates, and two calcium ions. Lignin peroxidase shows the typical, peroxidase fold and the heme has a close environment as found in other, peroxidases. During refinement of the LiP model an unprecedented, modification of an amino acid was recognized. The surface residue, tryptophan 171 in LiP is stereospecifically hydroxylated at the Cbeta atom, due to an autocatalytic process. We propose that during the catalytic, cycle of LiP a transient radical at Trp171 occurs that is different ... [(full description)]
About this Structure
1QPA is a [Single protein] structure of sequence from [Basidiomycete phanerochaete chrysosporium] with NAG, MAN, CA and HEM as [ligands]. Structure known Active Site: HE3. Full crystallographic information is available from [OCA].
Reference
The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle., Choinowski T, Blodig W, Winterhalter KH, Piontek K, J Mol Biol. 1999 Feb 26;286(3):809-27. PMID:10024453
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