2ih9
From Proteopedia
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|PDB= 2ih9 |SIZE=350|CAPTION= <scene name='initialview01'>2ih9</scene>, resolution 2.000Å | |PDB= 2ih9 |SIZE=350|CAPTION= <scene name='initialview01'>2ih9</scene>, resolution 2.000Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=5AX:2-(ACETYLAMINO)-1,5-ANHYDRO-2-DEOXY-D-GLUCITOL'>5AX</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Laccase Laccase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Laccase Laccase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] </span> |
|GENE= LAC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204285 Melanocarpus albomyces]) | |GENE= LAC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204285 Melanocarpus albomyces]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1gw0|1GW0]], [[2ih8|2IH8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ih9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ih9 OCA], [http://www.ebi.ac.uk/pdbsum/2ih9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ih9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Hakulinen, N.]] | [[Category: Hakulinen, N.]] | ||
[[Category: Rouvinen, J.]] | [[Category: Rouvinen, J.]] | ||
| - | [[Category: 5AX]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: SO4]] | ||
[[Category: laccase]] | [[Category: laccase]] | ||
[[Category: multicopper oxidase]] | [[Category: multicopper oxidase]] | ||
[[Category: redox enzyme]] | [[Category: redox enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:44:17 2008'' |
Revision as of 00:44, 31 March 2008
| |||||||
| , resolution 2.000Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Gene: | LAC1 (Melanocarpus albomyces) | ||||||
| Activity: | Laccase, with EC number 1.10.3.2 | ||||||
| Related: | 1GW0, 2IH8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A high-dose crystal structure of a recombinant Melanocarbus albomyces laccase
Overview
Laccases (p-diphenol dioxygen oxidoreductases) belong to the family of blue multicopper oxidases, which catalyse the four-electron reduction of dioxygen to water concomitantly through the oxidation of substrate molecules. Blue multicopper oxidases have four coppers, a copper (T1) forming a mononuclear site and a cluster of three coppers (T2, T3, and T3') forming a trinuclear site. Because X-rays are known to liberate electrons during data collection and may thus affect the oxidation state of metals, we have investigated the effect of X-ray radiation upon the crystal structure of a recombinant laccase from Melanocarpus albomyces through the use of crystallography and crystal absorption spectroscopy. Two data sets with different strategies, a low and a high-dose data set, were collected at synchrotron. We have observed earlier that the trinuclear site had an elongated electron density amidst coppers, suggesting dioxygen binding. The low-dose synchrotron structure showed similar elongated electron density, but the high-dose X-ray radiation removed the bulk of this density. Therefore, X-ray radiation could alter the active site of laccase from M. albomyces. Absorption spectra of the crystals (320, 420, and 590nm) during X-ray radiation were measured at a home laboratory. Spectra clearly showed how that the band at 590nm had vanished, resulting from the T1 copper being reduced, during the long X-ray measurements. The crystal colour changed from blue to colourless. Absorptions at 320 and 420nm seemed to be rather permanent. The absorption at 320nm is due to the T3 coppers and it is proposed that absorption at 420nm is due to the T2 copper when dioxygen or a reaction intermediate is close to this copper.
About this Structure
2IH9 is a Single protein structure of sequence from Melanocarpus albomyces. Full crystallographic information is available from OCA.
Reference
A crystallographic and spectroscopic study on the effect of X-ray radiation on the crystal structure of Melanocarpus albomyces laccase., Hakulinen N, Kruus K, Koivula A, Rouvinen J, Biochem Biophys Res Commun. 2006 Dec 1;350(4):929-34. Epub 2006 Oct 5. PMID:17045575
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