1v10: Difference between revisions
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[[Image:1v10.gif|left|200px]]<br /><applet load="1v10" size=" | [[Image:1v10.gif|left|200px]]<br /><applet load="1v10" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1v10, resolution 1.7Å" /> | caption="1v10, resolution 1.7Å" /> | ||
'''STRUCTURE OF RIGIDOPORUS LIGNOSUS LACCASE FROM HEMIHEDRALLY TWINNED CRYSTALS'''<br /> | '''STRUCTURE OF RIGIDOPORUS LIGNOSUS LACCASE FROM HEMIHEDRALLY TWINNED CRYSTALS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1V10 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rigidoporus_microporus Rigidoporus microporus] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Cu Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | 1V10 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rigidoporus_microporus Rigidoporus microporus] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Cu+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V10 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: oxidase]] | [[Category: oxidase]] | ||
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Revision as of 11:16, 3 February 2008
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STRUCTURE OF RIGIDOPORUS LIGNOSUS LACCASE FROM HEMIHEDRALLY TWINNED CRYSTALS
OverviewOverview
Laccase is a multicopper blue oxidase that couples the four-electron, reduction of oxygen with the oxidation of a broad range of organic, substrates, including phenols and arylamines. The enzyme is the object of, intense biotechnological research, due to its employment in bioremediation, of soils and water as well as in other biotechnological applications. We, report here the cDNA and protein sequences, the post-translational, modifications, the crystallization and X-ray structure determination of a, laccase from the white-rot fungus Rigidoporus lignosus. The amino acid, residues sequence deduced from cDNA clearly identified a pre-sequence of, 21 residues representing the signal for extra-cellular localization. Mass, spectrometry analysis performed on the salvage enzyme, confirmed the, deduced sequence and precisely mapped two glycosylation sites at Asn337, and Asn435, determining the nature of the bound glycosidic moieties. The, crystal structure was determined at 1.7A resolution from perfectly, hemihedrally twinned crystals, by molecular replacement technique. While, the overall structure closely resembled those reported for other fungal, laccases, the analysis of the T2/T3 trinuclear cluster revealed an, unprecedented coordination sphere for the T3 copper pair. No bridging, oxygen ligand was present between the two T3 copper ions, which were no, longer symmetrically coordinated. The observed structure could represent, an intermediate along the process of four-electron reduction of oxygen to, water taking place at the trinuclear copper cluster.
About this StructureAbout this Structure
1V10 is a Single protein structure of sequence from Rigidoporus microporus with as ligand. Active as Laccase, with EC number 1.10.3.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
The structure of Rigidoporus lignosus Laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair., Garavaglia S, Cambria MT, Miglio M, Ragusa S, Iacobazzi V, Palmieri F, D'Ambrosio C, Scaloni A, Rizzi M, J Mol Biol. 2004 Oct 1;342(5):1519-31. PMID:15364578
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