View source for 9lz9


==Reductive-half reaction intermediate of copper amine oxidase from Arthrobacter globiformis captured with short-a-axis diffraction data by mix-and-inject serial crystallography at 25-ms time delay==
<StructureSection load='9lz9' size='340' side='right'caption='[[9lz9]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9lz9]] 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=9LZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LZ9 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]] 2.13&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2TY:2-HYDROXY-5-{[(1E)-2-PHENYLETHYLIDENE]AMINO}-L-TYROSINE'>2TY</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=9lz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9lz9 OCA], [https://pdbe.org/9lz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9lz9 RCSB], [https://www.ebi.ac.uk/pdbsum/9lz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9lz9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PAOX_ARTGO PAOX_ARTGO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein dynamics play a crucial role in various physiological functions, including enzyme catalysis. To explore conformational changes during enzyme catalysis, we conduct mix-and-inject serial crystallography, an advanced technique to capture time-resolved protein structures in real time, using the microcrystals of bacterial copper amine oxidase containing a protein-derived quinone cofactor. Within 50 ms of mixing the microcrystals (&lt;4 mum) with a preferred substrate (2-phenylethylamine) under anaerobic conditions (reductive half-reaction), we observe domain movements associated with substrate binding and formation of a metastable reaction intermediate, a product Schiff-base of the quinone cofactor. At 100-1000 ms after mixing, conformational transition from aminoresorcinol to the semiquinone radical forms of the reduced cofactor progresses gradually, likely depending on the replacement of the product aldehyde by the next-cycle amine substrate that triggers the cofactor conformational change. Overall, this study provides structural insight into enzyme catalysis accompanying the active-site conformational changes that are hardly scrutinized by studies in solution.

Real-time capture of domain movements during copper amine oxidase catalysis by mix-and-inject serial crystallography.,Murakawa T, Suzuki M, Fukui K, Masuda T, Mizohata E, Miyahara I, Kurauchi I, Murakami T, Matsunaga H, Montawa Y, Nakajima N, Oozeki T, Sakai K, Son T, Higuchi T, Sunami T, Kimura T, Tono K, Tanaka T, Sugahara M, Arima T, Fangjia L, Kang J, Tanaka R, Iwata S, Nango E, Tosha T, Yano T, Tanizawa K, Okajima T Nat Commun. 2025 Dec 18;16(1):11149. doi: 10.1038/s41467-025-67230-5. PMID:41413268<ref>PMID:41413268</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9lz9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Arthrobacter globiformis]]
[[Category: Large Structures]]
[[Category: Murakawa T]]
[[Category: Okajima T]]