4ef3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:49, 20 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Multicopper Oxidase CueO (Citrate buffer)==
==Multicopper Oxidase CueO (Citrate buffer)==
-
<StructureSection load='4ef3' size='340' side='right' caption='[[4ef3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+
<StructureSection load='4ef3' size='340' side='right'caption='[[4ef3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4ef3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EF3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EF3 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4ef3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EF3 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cueO, yacK, b0123, JW0119 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ef3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ef3 OCA], [http://pdbe.org/4ef3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ef3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ef3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ef3 ProSAT]</span></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=4ef3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ef3 OCA], [https://pdbe.org/4ef3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ef3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ef3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ef3 ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/CUEO_ECOLI CUEO_ECOLI]
-
The acetate-bound form of the type II copper was found in the X-ray structure of the multicopper oxidase CueO crystallized in acetate buffer in addition to the conventional OH(-)-bound form as the major resting form. The acetate ion was retained bound to the type II copper even after prolonged exposure of a CueO crystal to X-ray radiation, which led to the stepwise reduction of the Cu centres. However, in this study, when CueO was crystallized in citrate buffer the OH(-)-bound form was present exclusively. This fact shows that an exogenous acetate ion reaches the type II Cu centre through the water channel constructed between domains 1 and 3 in the CueO molecule. It was also found that the enzymatic activity of CueO is enhanced in the presence of acetate ions in the solvent water.
+
-
 
+
-
Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity.,Komori H, Kataoka K, Tanaka S, Matsuda N, Higuchi Y, Sakurai T Acta Crystallogr F Struct Biol Commun. 2016 Jul 1;72(Pt 7):558-63. doi:, 10.1107/S2053230X16009237. Epub 2016 Jun 22. PMID:27380373<ref>PMID:27380373</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4ef3" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
-
*[[Blue copper oxidase CueO|Blue copper oxidase CueO]]
+
*[[Blue copper oxidase CueO 3D structures|Blue copper oxidase CueO 3D structures]]
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Ecoli]]
+
[[Category: Escherichia coli K-12]]
-
[[Category: Higuchi, Y]]
+
[[Category: Large Structures]]
-
[[Category: Kataoka, K]]
+
[[Category: Higuchi Y]]
-
[[Category: Komori, H]]
+
[[Category: Kataoka K]]
-
[[Category: Sakurai, T]]
+
[[Category: Komori H]]
-
[[Category: Metal binding protein]]
+
[[Category: Sakurai T]]
-
[[Category: Multicopper oxidase]]
+

Current revision

Multicopper Oxidase CueO (Citrate buffer)

PDB ID 4ef3

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ef3"
Personal tools