6l8d

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'''Unreleased structure'''
 
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The entry 6l8d is ON HOLD until Paper Publication
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==Hexameric structure of the ATPase subunit of magnesium chelatase==
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<StructureSection load='6l8d' size='340' side='right'caption='[[6l8d]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6l8d]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Syny3 Syny3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L8D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6L8D FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">chlI, slr1030 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1111708 SYNY3])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Magnesium_chelatase Magnesium chelatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.6.1.1 6.6.1.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6l8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l8d OCA], [http://pdbe.org/6l8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l8d RCSB], [http://www.ebi.ac.uk/pdbsum/6l8d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l8d ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CHLI_SYNY3 CHLI_SYNY3]] Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Magnesium chelatase (MgCh) is a heterotrimeric enzyme complex, composed of two AAA+ family subunits that can assembly into a double ring structure and a large catalytic subunit. The small AAA+ subunit has ATPase activity and can self-oligomerize into a ring structure, while the other AAA+ subunit lacks independent ATPase activity. Previous structural studies of the ATPase motor subunit of MgCh from a bacteriochlorophyll-synthesizing bacterium have identified a unique ATPase clade, but the model of oligomeric assembly is unclear. Here we present the hexameric structure of the MgCh ATPase motor subunit from the chlorophyll-synthesizing cyanobacterium Synechocystis sp. PCC 6803. This structure reveals details of how the hexameric ring is assembled, and thus provides a basis for further studying the heterotrimeric complex.
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Authors:
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Hexameric structure of the ATPase motor subunit of magnesium chelatase in chlorophyll biosynthesis.,Gao YS, Wang YL, Wang X, Liu L Protein Sci. 2020 Apr;29(4):1040-1046. doi: 10.1002/pro.3816. Epub 2020 Jan 7. PMID:31891428<ref>PMID:31891428</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 6l8d" 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: Magnesium chelatase]]
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[[Category: Syny3]]
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[[Category: Gao, Y]]
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[[Category: Liu, L]]
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[[Category: Aaa+]]
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[[Category: Atpase]]
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[[Category: Chlorophyll biosynthesis]]
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[[Category: Hydrolase]]

Revision as of 07:17, 8 April 2020

Hexameric structure of the ATPase subunit of magnesium chelatase

PDB ID 6l8d

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