9vwb
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==HamA, a Heme-Oxygenase-Like Enzyme== | |
| + | <StructureSection load='9vwb' size='340' side='right'caption='[[9vwb]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9vwb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_H111 Burkholderia cenocepacia H111]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VWB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VWB 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]] 2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=9vwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vwb OCA], [https://pdbe.org/9vwb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vwb RCSB], [https://www.ebi.ac.uk/pdbsum/9vwb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vwb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A144VC93_9BURK A0A144VC93_9BURK] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The fungicide fragin, which contains a diazeniumdiolate moiety, exhibits a broad spectrum of biological activities. HamA, the key enzyme responsible for forming the nitrogen-nitrogen bond in this moiety, was investigated in this study. We determined the crystal structure of HamA at 2.0 A resolution, revealing a mononuclear iron center in the active site coordinated by both the "2His-1Glu" motif and an acetate group. Notably, HamA adopts a heme oxygenase-like fold, forming a hydrophobic cavity within a helical bundle that likely accommodates the substrate. Structural data confirmed the presence of an acetate and a formate group near the active site and microscale thermophoresis (MST) experiments further demonstrated HamA's ability to bind 2-oxoglutarate (2OG) with a dissociation constant (K (d)) of 208 +/- 1.42 muM. In summary, this study elucidates the 2OG-dependent heme-oxygenase-like enzyme HamA with a monoiron active center, providing critical structural insights into the mechanistic formation of the diazeniumdiolate moiety in fragin. | ||
| - | + | Structural basis of a 2-oxoglutarate-dependent heme-oxygenase-like enzyme HamA in fragin biosynthesis.,Su B, Zhang T, Yu Y, Liu H RSC Adv. 2025 Oct 15;15(46):38502-38509. doi: 10.1039/d5ra05203c. eCollection , 2025 Oct 14. PMID:41103923<ref>PMID:41103923</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9vwb" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Burkholderia cenocepacia H111]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Liu HP]] | ||
| + | [[Category: Su BB]] | ||
| + | [[Category: Yu Y]] | ||
| + | [[Category: Zhang TT]] | ||
Current revision
HamA, a Heme-Oxygenase-Like Enzyme
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