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| | <StructureSection load='6ysg' size='340' side='right'caption='[[6ysg]], [[Resolution|resolution]] 2.54Å' scene=''> | | <StructureSection load='6ysg' size='340' side='right'caption='[[6ysg]], [[Resolution|resolution]] 2.54Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ysg]] is a 2 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=6YSG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YSG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ysg]] is a 2 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=6YSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YSG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></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]] 2.54Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6ys9|6ys9]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">chlH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1111708 SYNY3])</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=6ysg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ysg OCA], [https://pdbe.org/6ysg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ysg RCSB], [https://www.ebi.ac.uk/pdbsum/6ysg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ysg 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=6ysg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ysg OCA], [http://pdbe.org/6ysg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ysg RCSB], [http://www.ebi.ac.uk/pdbsum/6ysg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ysg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/P73020_SYNY3 P73020_SYNY3] |
| | <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: Syny3]] | + | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] |
| - | [[Category: Bisson, C]] | + | [[Category: Bisson C]] |
| - | [[Category: Hunter, C N]] | + | [[Category: Hunter CN]] |
| - | [[Category: Chlorophyll]]
| + | |
| - | [[Category: Magnesium chelatase]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| Structural highlights
Function
P73020_SYNY3
Publication Abstract from PubMed
The insertion of magnesium into protoporphyrin initiates the biosynthesis of chlorophyll, the pigment that underpins photosynthesis. This reaction, catalysed by the magnesium chelatase complex, couples ATP hydrolysis by a ChlID motor complex to chelation within the ChlH subunit. We probed the structure and catalytic function of ChlH using a combination of X-ray crystallography, computational modelling, mutagenesis and enzymology. Two linked domains of ChlH in an initially open conformation of ChlH bind protoporphyrin IX, and the rearrangement of several loops envelops this substrate, forming an active site cavity. This induced fit brings an essential glutamate (E660), proposed to be the key catalytic residue for magnesium insertion, into proximity with the porphyrin. A buried solvent channel adjacent to E660 connects the exterior bulk solvent to the active site, forming a possible conduit for the delivery of magnesium or abstraction of protons.
The active site of magnesium chelatase.,Adams NBP, Bisson C, Brindley AA, Farmer DA, Davison PA, Reid JD, Hunter CN Nat Plants. 2020 Nov 30. pii: 10.1038/s41477-020-00806-9. doi:, 10.1038/s41477-020-00806-9. PMID:33257858[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Adams NBP, Bisson C, Brindley AA, Farmer DA, Davison PA, Reid JD, Hunter CN. The active site of magnesium chelatase. Nat Plants. 2020 Nov 30. pii: 10.1038/s41477-020-00806-9. doi:, 10.1038/s41477-020-00806-9. PMID:33257858 doi:http://dx.doi.org/10.1038/s41477-020-00806-9
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