6nte

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'''Unreleased structure'''
 
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The entry 6nte is ON HOLD until Paper Publication
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==Crystal Structure of Synechocystis Dihydroxyacid Dehydratase (DHAD)==
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<StructureSection load='6nte' size='340' side='right'caption='[[6nte]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6nte]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NTE 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]] 2.33&#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=6nte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nte OCA], [https://pdbe.org/6nte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nte RCSB], [https://www.ebi.ac.uk/pdbsum/6nte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nte ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ILVD_SYNY3 ILVD_SYNY3]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Microbes are essential to the global ecosystem, but undesirable microbial growth causes issues ranging from food spoilage and infectious diseases to harmful cyanobacterial blooms. The use of chemicals to control microbial growth has achieved significant success, while specific roles for a majority of essential genes in growth control remain unexplored. Here, we show the growth inhibition of cyanobacterial species by targeting an essential enzyme for the biosynthesis of branched-chain amino acids. Specifically, we report the biochemical, genetic, and structural characterization of dihydroxyacid dehydratase from the model cyanobacterium Synechocystis sp. PCC 6803 (SnDHAD). Our studies suggest that SnDHAD is an oxygen-stable enzyme containing a [2Fe-2S] cluster. Furthermore, we demonstrate that SnDHAD is selectively inhibited in vitro and in vivo by the natural product aspterric acid, which also inhibits the growth of representative bloom-forming Microcystis and Anabaena strains but has minimal effects on microbial pathogens with [4Fe-4S] containing DHADs. This study suggests DHADs as a promising target for the precise growth control of microbes and highlights the exploration of other untargeted essential genes for microbial management.
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Authors:
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Cyanobacterial Dihydroxyacid Dehydratases Are a Promising Growth Inhibition Target.,Zhang P, MacTavish BS, Yang G, Chen M, Roh J, Newsome KR, Bruner SD, Ding Y ACS Chem Biol. 2020 Aug 21;15(8):2281-2288. doi: 10.1021/acschembio.0c00507. Epub, 2020 Aug 12. PMID:32786290<ref>PMID:32786290</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 6nte" 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: Large Structures]]
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[[Category: Synechocystis sp. PCC 6803]]
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[[Category: Bruner S]]
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[[Category: MacTavish B]]

Current revision

Crystal Structure of Synechocystis Dihydroxyacid Dehydratase (DHAD)

PDB ID 6nte

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