1lyc
From Proteopedia
(New page: 200px<br /><applet load="1lyc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lyc, resolution 1.57Å" /> '''The impact of the ph...) |
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| - | [[Image:1lyc.jpg|left|200px]]<br /><applet load="1lyc" size=" | + | [[Image:1lyc.jpg|left|200px]]<br /><applet load="1lyc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lyc, resolution 1.57Å" /> | caption="1lyc, resolution 1.57Å" /> | ||
'''The impact of the physical and chemical enviroment on the molecular structure of Coprinus cinereus peroxidase'''<br /> | '''The impact of the physical and chemical enviroment on the molecular structure of Coprinus cinereus peroxidase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the peroxidase from Coprinus cinereus (CiP) has been | + | The structure of the peroxidase from Coprinus cinereus (CiP) has been determined in three different space groups and crystalline environments. Two of these are of the recombinant glycosylated form (rCiP), which crystallized in space groups P2(1)2(1)2(1) and C2. The third crystal form was obtained from a variant of CiP in which the glycosylation sites have been removed (rCiPON). It crystallizes in space group P2(1) with beta approximately 90 degrees; the structure was determined from room-temperature data and low-temperature data obtained from twinned crystals. Two independent molecules of CiP related by non-crystallographic symmetry are contained in the three crystal forms. The packing in the two structures of the glycosylated form of rCiP is closely related, but differs from the packing in the unglycosylated rCiPON. A database search based on small-molecule porphinato iron (III) complexes has been performed and related to observations of the spin states and coordination numbers of the iron ion. The room-temperature structures of CiP and one structure of the almost identical peroxidase from Arthromyces ramosus (ARP) have been used to identify 66 conserved water molecules and to assign a structural role to most of them. |
==About this Structure== | ==About this Structure== | ||
| - | 1LYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea] with CA and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http:// | + | 1LYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LYC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Houborg, K.]] | [[Category: Houborg, K.]] | ||
[[Category: Larsen, S.]] | [[Category: Larsen, S.]] | ||
| - | [[Category: Petersen, J | + | [[Category: Petersen, J F.W.]] |
| - | [[Category: Poulsen, J | + | [[Category: Poulsen, J C.N.]] |
[[Category: Rowland, P.]] | [[Category: Rowland, P.]] | ||
[[Category: Schneider, P.]] | [[Category: Schneider, P.]] | ||
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[[Category: thermostability]] | [[Category: thermostability]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:32 2008'' |
Revision as of 11:49, 21 February 2008
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The impact of the physical and chemical enviroment on the molecular structure of Coprinus cinereus peroxidase
Overview
The structure of the peroxidase from Coprinus cinereus (CiP) has been determined in three different space groups and crystalline environments. Two of these are of the recombinant glycosylated form (rCiP), which crystallized in space groups P2(1)2(1)2(1) and C2. The third crystal form was obtained from a variant of CiP in which the glycosylation sites have been removed (rCiPON). It crystallizes in space group P2(1) with beta approximately 90 degrees; the structure was determined from room-temperature data and low-temperature data obtained from twinned crystals. Two independent molecules of CiP related by non-crystallographic symmetry are contained in the three crystal forms. The packing in the two structures of the glycosylated form of rCiP is closely related, but differs from the packing in the unglycosylated rCiPON. A database search based on small-molecule porphinato iron (III) complexes has been performed and related to observations of the spin states and coordination numbers of the iron ion. The room-temperature structures of CiP and one structure of the almost identical peroxidase from Arthromyces ramosus (ARP) have been used to identify 66 conserved water molecules and to assign a structural role to most of them.
About this Structure
1LYC is a Single protein structure of sequence from Coprinopsis cinerea with and as ligands. Active as Peroxidase, with EC number 1.11.1.7 Full crystallographic information is available from OCA.
Reference
Impact of the physical and chemical environment on the molecular structure of Coprinus cinereus peroxidase., Houborg K, Harris P, Petersen J, Rowland P, Poulsen JC, Schneider P, Vind J, Larsen S, Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):989-96. Epub 2003, May 23. PMID:12777760
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