6yt0: Difference between revisions
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==Magnesium chelatase H subunit (ChlH) E660D variant from Synechocystis sp.PCC6803== | |||
<StructureSection load='6yt0' size='340' side='right'caption='[[6yt0]], [[Resolution|resolution]] 2.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6yt0]] 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=6YT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YT0 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]] 2.85Å</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=6yt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yt0 OCA], [https://pdbe.org/6yt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yt0 RCSB], [https://www.ebi.ac.uk/pdbsum/6yt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yt0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/P73020_SYNY3 P73020_SYNY3] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:33257858</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6yt0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] | |||
[[Category: Bisson C]] | |||
[[Category: Hunter CN]] | |||
Latest revision as of 16:34, 24 January 2024
Magnesium chelatase H subunit (ChlH) E660D variant from Synechocystis sp.PCC6803Magnesium chelatase H subunit (ChlH) E660D variant from Synechocystis sp.PCC6803
Structural highlights
FunctionPublication Abstract from PubMedThe 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
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