3s1e

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<StructureSection load='3s1e' size='340' side='right'caption='[[3s1e]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3s1e' size='340' side='right'caption='[[3s1e]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3s1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Maize Maize]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S1E FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3s1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S1E FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZIP:N-(3-METHYLBUT-2-EN-1-YL)-9H-PURIN-6-AMINE'>ZIP</scene></td></tr>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bw7|3bw7]], [[3c0p|3c0p]], [[2qkn|2qkn]], [[1w1q|1w1q]], [[3dq0|3dq0]], [[1w1r|1w1r]], [[1w1s|1w1s]], [[2qpm|2qpm]], [[3kjm|3kjm]], [[3s1c|3s1c]], [[3s1d|3s1d]], [[3s1f|3s1f]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZIP:N-(3-METHYLBUT-2-EN-1-YL)-9H-PURIN-6-AMINE'>ZIP</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CKX1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4577 MAIZE])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cytokinin_dehydrogenase Cytokinin dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.99.12 1.5.99.12] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3s1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s1e OCA], [https://pdbe.org/3s1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s1e RCSB], [https://www.ebi.ac.uk/pdbsum/3s1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s1e 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=3s1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s1e OCA], [https://pdbe.org/3s1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s1e RCSB], [https://www.ebi.ac.uk/pdbsum/3s1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s1e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CKX1_MAIZE CKX1_MAIZE]] Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group. Cleaves zeatin, isopentenyladenine, isopentenyladenosine, zeatin riboside and cis-zeatin, but not dihydrozeatin, kinetin and benzylaminopurine.
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[https://www.uniprot.org/uniprot/CKX1_MAIZE CKX1_MAIZE] Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group. Cleaves zeatin, isopentenyladenine, isopentenyladenosine, zeatin riboside and cis-zeatin, but not dihydrozeatin, kinetin and benzylaminopurine.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cytokinins are hormones that regulate plant development and their environmental responses. Their levels are mainly controlled by the cytokinin oxidase/dehydrogenase (CKO), which oxidatively cleaves cytokinins using redox-active electron acceptors. CKO belongs to the group of flavoproteins with an 8alpha-N1-histidyl FAD covalent linkage. Here, we investigated the role of seven active site residues: H105, D169, E288, V378, E381, P427 and L492, in substrate binding and catalysis of the CKO1 from maize (Zea mays, ZmCKO1) combining site-directed mutagenesis with kinetics and X-ray crystallography. Here, we identify E381 as a key residue for enzyme specificity that restricts substrate binding as well as quinone electron acceptor binding. We show that D169 is important for catalysis and that H105 covalently linked to FAD maintains the enzyme's structural integrity, stability and high rates with electron acceptors. The L492A mutation significantly modulates the cleavage of aromatic cytokinins and zeatin isomers. The high resolution X-ray structures of ZmCKO1 and the E381S variant in complex with N6-(2-isopentenyl)adenosine (iPR) reveal the binding mode of cytokinin ribosides. Those of ZmCKO2 and ZmCKO4a contain a mobile domain, which might contribute to binding of the N9 substituted cytokinins. This article is protected by copyright. All rights reserved.
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Kinetic and structural investigation of the cytokinin oxidase/dehydrogenase active site.,Kopecny D, Koncitikova R, Popelka H, Briozzo P, Vigouroux A, Kopecna M, Zalabak D, Sebela M, Skopalova J, Frebort I, Morera S FEBS J. 2015 Oct 31. doi: 10.1111/febs.13581. PMID:26519657<ref>PMID:26519657</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3s1e" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cytokinin dehydrogenase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Maize]]
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[[Category: Zea mays]]
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[[Category: Briozzo, P]]
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[[Category: Briozzo P]]
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[[Category: Kopecny, D]]
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[[Category: Kopecny D]]
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[[Category: Morera, S]]
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[[Category: Morera S]]
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[[Category: Covalent flavination]]
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[[Category: Cytokinin binding]]
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[[Category: Cytokinin oxidase/dehydrogenase]]
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[[Category: Fad binding protein]]
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[[Category: Flavoprotein]]
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[[Category: Glycosylation]]
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[[Category: Oxidoreductase]]
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Revision as of 12:43, 14 March 2024

Pro427Gln mutant of maize cytokinin oxidase/dehydrogenase complexed with N6-isopentenyladenine

PDB ID 3s1e

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