6yt0: Difference between revisions

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<StructureSection load='6yt0' size='340' side='right'caption='[[6yt0]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='6yt0' size='340' side='right'caption='[[6yt0]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6yt0]] 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=6YT0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YT0 FirstGlance]. <br>
<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6ysg|6ysg]], [[6ys9|6ys9]]</div></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]] 2.85&#8491;</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=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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6yt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yt0 OCA], [http://pdbe.org/6yt0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yt0 RCSB], [http://www.ebi.ac.uk/pdbsum/6yt0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yt0 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]]

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

6yt0 is a 2 chain structure with sequence from Synechocystis sp. PCC 6803 substr. Kazusa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.85Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. 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

6yt0, resolution 2.85Å

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OCA