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| | <StructureSection load='6l8d' size='340' side='right'caption='[[6l8d]], [[Resolution|resolution]] 2.91Å' scene=''> | | <StructureSection load='6l8d' size='340' side='right'caption='[[6l8d]], [[Resolution|resolution]] 2.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <table><tr><td colspan='2'>[[6l8d]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6L8D FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.91Å</td></tr> |
| - | <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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6l8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l8d OCA], [https://pdbe.org/6l8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l8d RCSB], [https://www.ebi.ac.uk/pdbsum/6l8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l8d ProSAT]</span></td></tr> |
| - | <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> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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. | + | [https://www.uniprot.org/uniprot/CHLI_SYNY3 CHLI_SYNY3] Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Magnesium chelatase]] | + | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] |
| - | [[Category: Syny3]]
| + | [[Category: Gao Y]] |
| - | [[Category: Gao, Y]] | + | [[Category: Liu L]] |
| - | [[Category: Liu, L]] | + | |
| - | [[Category: Aaa+]]
| + | |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Chlorophyll biosynthesis]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
CHLI_SYNY3 Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gao YS, Wang YL, Wang X, Liu L. Hexameric structure of the ATPase motor subunit of magnesium chelatase in chlorophyll biosynthesis. Protein Sci. 2020 Apr;29(4):1040-1046. doi: 10.1002/pro.3816. Epub 2020 Jan 7. PMID:31891428 doi:http://dx.doi.org/10.1002/pro.3816
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