View source for 5zpe


==Copper amine oxidase from Arthrobacter globiformis anaerobically reduced by ethylamine at pH 6 at 288 K (2)==
<StructureSection load='5zpe' size='340' side='right'caption='[[5zpe]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zpe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZPE 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]] 1.689&#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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TYQ:3-AMINO-6-HYDROXY-TYROSINE'>TYQ</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=5zpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zpe OCA], [https://pdbe.org/5zpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zpe RCSB], [https://www.ebi.ac.uk/pdbsum/5zpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zpe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PAOX_ARTGO PAOX_ARTGO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the catalytic reaction of copper amine oxidase, the protein-derived redox cofactor topaquinone (TPQ) is reduced by an amine substrate to an aminoresorcinol form (TPQamr), which is in equilibrium with a semiquinone radical (TPQsq). The transition from TPQamr to TPQsq is an endothermic process, accompanied by a significant conformational change of the cofactor. We employed the humid air and glue-coating (HAG) method to capture the equilibrium mixture of TPQamr and TPQsq in noncryocooled crystals of the enzyme from Arthrobacter globiformis and found that the equilibrium shifts more toward TPQsq in crystals than in solution. Thermodynamic analyses of the temperature-dependent equilibrium also revealed that the transition to TPQsq is entropy-driven both in crystals and in solution, giving the thermodynamic parameters that led to experimental determination of the crystal packing effect. Furthermore, we demonstrate that the binding of product aldehyde to the hydrophobic pocket in the active site produces various equilibrium states among two forms of the product Schiff-base, TPQamr, and TPQsq, in a pH-dependent manner. The temperature-controlled HAG method provides a technique for thermodynamic analysis of conformational changes occurring in protein crystals that are hardly scrutinized by conventional cryogenic X-ray crystallography.

In crystallo thermodynamic analysis of conformational change of the topaquinone cofactor in bacterial copper amine oxidase.,Murakawa T, Baba S, Kawano Y, Hayashi H, Yano T, Kumasaka T, Yamamoto M, Tanizawa K, Okajima T Proc Natl Acad Sci U S A. 2018 Dec 18. pii: 1811837116. doi:, 10.1073/pnas.1811837116. PMID:30563857<ref>PMID:30563857</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zpe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arthrobacter globiformis]]
[[Category: Large Structures]]
[[Category: Baba S]]
[[Category: Hayashi H]]
[[Category: Kawano Y]]
[[Category: Kumasaka T]]
[[Category: Murakawa T]]
[[Category: Okajima T]]
[[Category: Tanizawa K]]
[[Category: Yamamoto M]]
[[Category: Yano T]]