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| | <StructureSection load='6uyk' size='340' side='right'caption='[[6uyk]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='6uyk' size='340' side='right'caption='[[6uyk]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6uyk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"luteovulum_sphaeroides"_(van_niel_1944)_suresh_et_al._2019 "luteovulum sphaeroides" (van niel 1944) suresh et al. 2019]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UYK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6uyk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UYK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bchL, RHOS4_18930, RSP_0288 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ferredoxin:protochlorophyllide_reductase_(ATP-dependent) Ferredoxin:protochlorophyllide reductase (ATP-dependent)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.7.7 1.3.7.7] </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=6uyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uyk OCA], [https://pdbe.org/6uyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uyk RCSB], [https://www.ebi.ac.uk/pdbsum/6uyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uyk ProSAT]</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=6uyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uyk OCA], [https://pdbe.org/6uyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uyk RCSB], [https://www.ebi.ac.uk/pdbsum/6uyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uyk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/BCHL_RHOS4 BCHL_RHOS4]] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.[HAMAP-Rule:MF_00355]<ref>PMID:19006326</ref>
| + | [https://www.uniprot.org/uniprot/BCHL_CERS4 BCHL_CERS4] Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.[HAMAP-Rule:MF_00355]<ref>PMID:19006326</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Cereibacter sphaeroides]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ando, N]] | + | [[Category: Ando N]] |
| - | [[Category: Antony, E]] | + | [[Category: Antony E]] |
| - | [[Category: Bacik, J P]] | + | [[Category: Bacik JP]] |
| - | [[Category: Corless, E]] | + | [[Category: Corless E]] |
| - | [[Category: Imran, S M.S]] | + | [[Category: Imran SMS]] |
| - | [[Category: Watkins, M B]] | + | [[Category: Watkins MB]] |
| - | [[Category: Dpor]]
| + | |
| - | [[Category: Electron transfer]]
| + | |
| - | [[Category: Iron-sulfur cluster]]
| + | |
| - | [[Category: Nitrogenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| Structural highlights
Function
BCHL_CERS4 Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.[HAMAP-Rule:MF_00355][1]
Publication Abstract from PubMed
A key step in bacteriochlorophyll biosynthesis is the reduction of protochlorophyllide to chlorophyllide, catalyzed by dark-operative protochlorophyllide oxidoreductase (DPOR). DPOR contains two [4Fe-4S]-containing component proteins (BchL and BchNB) that assemble upon ATP binding to BchL to coordinate electron transfer and protochlorophyllide reduction. But the precise nature of the ATP-induced conformational changes are poorly understood. We present a crystal structure of BchL in the nucleotide-free form where a conserved, flexible region in the N-terminus masks the [4Fe-4S] cluster at the docking interface between BchL and BchNB. Amino acid substitutions in this region produce a hyper-active enzyme complex, suggesting a role for the N-terminus in auto-inhibition. Hydrogen deuterium exchange mass spectrometry shows that ATP-binding to BchL produces specific conformational changes leading to release of the flexible N-terminus from the docking interface. The release also promotes changes within the local environment surrounding the [4Fe-4S] cluster and promotes BchL complex formation with BchNB. A key patch of amino acids, Asp-Phe-Asp (the 'DFD patch'), situated at the mouth of the BchL ATP-binding pocket promotes inter-subunit cross stabilization of the two subunits. A linked BchL dimer with one defective ATP-binding site does not support protochlorophyllide reduction, illustrating nucleotide binding to both subunits as a prerequisite for the inter-subunit cross stabilization. The masking of the [4Fe-4S] cluster by the flexible N-terminal region and the associated inhibition of activity is a novel mechanism of regulation in metalloproteins. Such mechanisms are possibly an adaptation to the anaerobic nature of eubacterial cells with poor tolerance for oxygen.
The flexible N-terminus of BchL autoinhibits activity through interaction with its [4Fe-4S] cluster and relieved upon ATP binding.,Corless EI, Saad Imran SM, Watkins MB, Bacik JP, Mattice J, Patterson A, Danyal K, Soffe M, Kitelinger R, Seefeldt LC, Origanti SS, Bennett B, Bothner B, Ando N, Antony E J Biol Chem. 2020 Nov 20:100107. doi: 10.1074/jbc.RA120.016278. PMID:33219127[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sarma R, Barney BM, Hamilton TL, Jones A, Seefeldt LC, Peters JW. Crystal Structure of the L Protein of Rhodobacter sphaeroides Light-Independent Protochlorophyllide Reductase with MgADP Bound: A Homologue of the Nitrogenase Fe Protein. Biochemistry. 2008 Nov 12. PMID:19006326 doi:10.1021/bi801058r
- ↑ Corless EI, Saad Imran SM, Watkins MB, Bacik JP, Mattice J, Patterson A, Danyal K, Soffe M, Kitelinger R, Seefeldt LC, Origanti SS, Bennett B, Bothner B, Ando N, Antony E. The flexible N-terminus of BchL autoinhibits activity through interaction with its [4Fe-4S] cluster and relieved upon ATP binding. J Biol Chem. 2020 Nov 20:100107. doi: 10.1074/jbc.RA120.016278. PMID:33219127 doi:http://dx.doi.org/10.1074/jbc.RA120.016278
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