2x31
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Modelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang== | |
| + | <SX load='2x31' size='340' side='right' viewer='molstar' caption='[[2x31]], [[Resolution|resolution]] 7.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == 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<ref>PMID:20223218</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2x31" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rhodobacter capsulatus]] | ||
| + | [[Category: Al-Karadaghi S]] | ||
| + | [[Category: Berglund L]] | ||
| + | [[Category: Elmlund D]] | ||
| + | [[Category: Elmlund H]] | ||
| + | [[Category: Emanuelsson C]] | ||
| + | [[Category: Hansson M]] | ||
| + | [[Category: Hebert H]] | ||
| + | [[Category: Lindahl M]] | ||
| + | [[Category: Lunqvist J]] | ||
| + | [[Category: Peterson Wulff R]] | ||
| + | [[Category: Willows RD]] | ||
Current revision
Modelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang
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