9ijf

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Current revision (18:05, 7 May 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9ijf is ON HOLD
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==Structure of ATP-dependent diazotase CmaA6==
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<StructureSection load='9ijf' size='340' side='right'caption='[[9ijf]], [[Resolution|resolution]] 2.73&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9ijf]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Kutzneria_albida_DSM_43870 Kutzneria albida DSM 43870]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9IJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9IJF FirstGlance]. <br>
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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]] 2.73&#8491;</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=9ijf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ijf OCA], [https://pdbe.org/9ijf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ijf RCSB], [https://www.ebi.ac.uk/pdbsum/9ijf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ijf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/W5W4E6_9PSEU W5W4E6_9PSEU]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Although several diazotases have been recently reported, the details of the reaction mechanism are not yet understood. In this study, we investigated the mechanism of CmaA6, an ATP-dependent diazotase, which catalyzes the diazotization of 3-aminocoumaric acid using nitrous acid. X-ray crystallography and cryogenic electron microscopy-single particle analysis revealed CmaA6 structures in the substrate-free and AMP-binding states. Kinetic analysis suggested that CmaA6 catalyzes diazotization via a sequential reaction mechanism in which three substrates (nitrous acid, ATP, and 3-aminocoumaric acid) are simultaneously bound in the reaction pocket. The nitrous acid and 3-aminocoumaric acid binding sites were predicted based on the AMP-binding state and confirmed by site-directed mutagenesis. In addition, computational analysis revealed a tunnel for 3-aminocoumaric acid to enter the reaction pocket, which was advantageous for the sequential reaction mechanism. This study provides important insights into the catalytic mechanism of diazotization in natural product biosynthesis.
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Authors:
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Structural Basis for the Catalytic Mechanism of ATP-Dependent Diazotase CmaA6.,Kawai S, Karasawa M, Moriwaki Y, Terada T, Katsuyama Y, Ohnishi Y Angew Chem Int Ed Engl. 2025 Apr 24:e202505851. doi: 10.1002/anie.202505851. PMID:40275441<ref>PMID:40275441</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9ijf" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Kutzneria albida DSM 43870]]
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[[Category: Large Structures]]
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[[Category: Katsuyama Y]]
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[[Category: Kawai S]]
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[[Category: Ohnishi Y]]

Current revision

Structure of ATP-dependent diazotase CmaA6

PDB ID 9ijf

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