This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1a65

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:47, 2 August 2023) (edit) (undo)
 
(21 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1a65.gif|left|200px]]<br />
 
-
<applet load="1a65" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1a65, resolution 2.23&Aring;" />
 
-
'''TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS'''<br />
 
-
==Overview==
+
==TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS==
-
Laccase catalyses the oxidation of a variety of organic substrates coupled, to the reduction of oxygen to water. It is widely believed to be the, simplest representative of the ubiquitous blue multi-copper oxidase, family. Laccase is implicated in a wide spectrum of biological activities, and, in particular, plays a key role in morphogenesis, development and, lignin metabolism in fungi and plants. The structure of laccase from the, fungus Coprinus cinereus has been determined by X-ray crystallography at a, resolution of 2.2 A. Laccase is a monomer composed of three, cupredoxin-like beta-sandwich domains, similar to that found in ascorbate, oxidase. In contrast to ascorbate oxidase, however, the mononuclear type-1, Cu site lacks the axial methionine ligand and so exhibits trigonal planar, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9546223 (full description)]]
+
<StructureSection load='1a65' size='340' side='right'caption='[[1a65]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1a65]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A65 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=PYE:TETRAHYDROPYRAN'>PYE</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a65 OCA], [https://pdbe.org/1a65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a65 RCSB], [https://www.ebi.ac.uk/pdbsum/1a65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a65 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q9Y780_COPCI Q9Y780_COPCI]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/1a65_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a65 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Laccase catalyses the oxidation of a variety of organic substrates coupled to the reduction of oxygen to water. It is widely believed to be the simplest representative of the ubiquitous blue multi-copper oxidase family. Laccase is implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. The structure of laccase from the fungus Coprinus cinereus has been determined by X-ray crystallography at a resolution of 2.2 A. Laccase is a monomer composed of three cupredoxin-like beta-sandwich domains, similar to that found in ascorbate oxidase. In contrast to ascorbate oxidase, however, the mononuclear type-1 Cu site lacks the axial methionine ligand and so exhibits trigonal planar coordination, consistent with its elevated redox potential. Crucially, the structure is trapped in a Cu depleted form in which the putative type-2 Cu atom is completely absent, but in which the remaining type-1 and type-3 Cu sites display full occupancy. Type-2 Cu depletion has unexpected consequences for the coordination of the remaining type-3 Cu atoms.
-
==About this Structure==
+
Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution.,Ducros V, Brzozowski AM, Wilson KS, Brown SH, Ostergaard P, Schneider P, Yaver DS, Pedersen AH, Davies GJ Nat Struct Biol. 1998 Apr;5(4):310-6. PMID:9546223<ref>PMID:9546223</ref>
-
1A65 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Coprinus_cinereus Coprinus cinereus]] with NAG, GLC, CU and O as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2]]. Structure known Active Sites: T1 and T3. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A65 OCA]].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution., Ducros V, Brzozowski AM, Wilson KS, Brown SH, Ostergaard P, Schneider P, Yaver DS, Pedersen AH, Davies GJ, Nat Struct Biol. 1998 Apr;5(4):310-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9546223 9546223]
+
</div>
-
[[Category: Coprinus cinereus]]
+
<div class="pdbe-citations 1a65" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Brzozowski, W.]]
+
-
[[Category: Ducros, V.]]
+
-
[[Category: CU]]
+
-
[[Category: GLC]]
+
-
[[Category: NAG]]
+
-
[[Category: O]]
+
-
[[Category: blue multi-copper oxidase]]
+
-
[[Category: glycoprotein]]
+
-
[[Category: laccase]]
+
-
[[Category: oxidoreductase]]
+
-
[[Category: signal]]
+
-
[[Category: type-2 copper depleted]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:48:21 2007''
+
==See Also==
 +
*[[Laccase 3D structures|Laccase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Coprinopsis cinerea]]
 +
[[Category: Large Structures]]
 +
[[Category: Brzozowski W]]
 +
[[Category: Ducros V]]

Current revision

TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS

PDB ID 1a65

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools