1gw0: Difference between revisions

Revision as of 06:11, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1gw0.png

Template:STRUCTURE 1gw0

CRYSTAL STRUCTURE OF LACCASE FROM MELANOCARPUS ALBOMYCES IN FOUR COPPER FORMCRYSTAL STRUCTURE OF LACCASE FROM MELANOCARPUS ALBOMYCES IN FOUR COPPER FORM

Template:ABSTRACT PUBMED 12118243

About this StructureAbout this Structure

1GW0 is a Single protein structure of sequence from Melanocarpus albomyces. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site., Hakulinen N, Kiiskinen LL, Kruus K, Saloheimo M, Paananen A, Koivula A, Rouvinen J, Nat Struct Biol. 2002 Aug;9(8):601-5. PMID:12118243

Page seeded by OCA on Tue Jul 1 06:11:40 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1gw0.jpg|left|200px]]
+{{Seed}}
+[[Image:1gw0.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1gw0|  PDB=1gw0  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF LACCASE FROM MELANOCARPUS ALBOMYCES IN FOUR COPPER FORM'''
+===CRYSTAL STRUCTURE OF LACCASE FROM MELANOCARPUS ALBOMYCES IN FOUR COPPER FORM===
-==Overview==
+<!--
-We have crystallized the ascomycete laccase from Melanocarpus albomyces with all four coppers present and determined the crystal structure at 2.4 A resolution. The enzyme is heavily glycosylated and consists of three cupredoxin-like domains, similar to those found in the Cu-depleted basidiomycete laccase from Coprinus cinereus. However, there are significant differences in the loops forming the substrate-binding pocket. In addition, the crystal structure of the M. albomyces laccase revealed elongated electron density between all three coppers in the trinuclear copper site, suggesting that an oxygen molecule binds with a novel geometry. This oxygen, required in the reaction, may enter the trinuclear site through the tunnel, which is open in the structure of the C. cinereus laccase. In contrast, the C-terminus on the M. albomyces laccase forms a plug that blocks this access.
+The line below this paragraph, {{ABSTRACT_PUBMED_12118243}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12118243 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12118243}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Multi-copper oxidase]]
 [[Category: Oxygen reduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:04:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:11:40 2008''