|
|
| (6 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Modelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang== | | ==Modelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang== |
| - | <StructureSection load='2x31' size='340' side='right' caption='[[2x31]], [[Resolution|resolution]] 7.50Å' scene=''> | + | <SX load='2x31' size='340' side='right' viewer='molstar' caption='[[2x31]], [[Resolution|resolution]] 7.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x31]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X31 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X31 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x31]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X31 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g8p|1g8p]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.5Å</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=2x31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x31 OCA], [https://pdbe.org/2x31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x31 RCSB], [https://www.ebi.ac.uk/pdbsum/2x31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x31 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x31 OCA], [http://pdbe.org/2x31 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x31 RCSB], [http://www.ebi.ac.uk/pdbsum/2x31 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x31 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BCHD_RHOCB BCHD_RHOCB]] Involved in bacteriochlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. [[http://www.uniprot.org/uniprot/BCHI_RHOCB BCHI_RHOCB]] Involved in bacteriochlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. | + | [https://www.uniprot.org/uniprot/BCHD_RHOCB BCHD_RHOCB] Involved in bacteriochlorophyll 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 == |
| Line 22: |
Line 21: |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Rhodonostoc capsulatum molisch 1907]] | + | [[Category: Large Structures]] |
| - | [[Category: Magnesium chelatase]] | + | [[Category: Rhodobacter capsulatus]] |
| - | [[Category: Al-Karadaghi, S]] | + | [[Category: Al-Karadaghi S]] |
| - | [[Category: Berglund, L]] | + | [[Category: Berglund L]] |
| - | [[Category: Elmlund, D]] | + | [[Category: Elmlund D]] |
| - | [[Category: Elmlund, H]] | + | [[Category: Elmlund H]] |
| - | [[Category: Emanuelsson, C]] | + | [[Category: Emanuelsson C]] |
| - | [[Category: Hansson, M]] | + | [[Category: Hansson M]] |
| - | [[Category: Hebert, H]] | + | [[Category: Hebert H]] |
| - | [[Category: Lindahl, M]] | + | [[Category: Lindahl M]] |
| - | [[Category: Lunqvist, J]] | + | [[Category: Lunqvist J]] |
| - | [[Category: Willows, R D]] | + | [[Category: Peterson Wulff R]] |
| - | [[Category: Wulff, R Peterson]]
| + | [[Category: Willows RD]] |
| - | [[Category: Bacteriochlorophyll biosynthesis]] | + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| Structural highlights
Function
BCHD_RHOCB Involved in bacteriochlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
Publication Abstract from PubMed
Mg-chelatase catalyzes the first committed step of the chlorophyll biosynthetic pathway, the ATP-dependent insertion of Mg(2+) into protoporphyrin IX (PPIX). Here we report the reconstruction using single-particle cryo-electron microscopy of the complex between subunits BchD and BchI of Rhodobacter capsulatus Mg-chelatase in the presence of ADP, the nonhydrolyzable ATP analog AMPPNP, and ATP at 7.5 A, 14 A, and 13 A resolution, respectively. We show that the two AAA+ modules of the subunits form a unique complex of 3 dimers related by a three-fold axis. The reconstructions demonstrate substantial differences between the conformations of the complex in the presence of ATP and ADP, and suggest that the C-terminal integrin-I domains of the BchD subunits play a central role in transmitting conformational changes of BchI to BchD. Based on these data a model for the function of magnesium chelatase is proposed.
ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase.,Lundqvist J, Elmlund H, Wulff RP, Berglund L, Elmlund D, Emanuelsson C, Hebert H, Willows RD, Hansson M, Lindahl M, Al-Karadaghi S Structure. 2010 Mar 10;18(3):354-65. PMID:20223218[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lundqvist J, Elmlund H, Wulff RP, Berglund L, Elmlund D, Emanuelsson C, Hebert H, Willows RD, Hansson M, Lindahl M, Al-Karadaghi S. ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase. Structure. 2010 Mar 10;18(3):354-65. PMID:20223218 doi:10.1016/j.str.2010.01.001
|
