2x31: Difference between revisions
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The | ==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]] | |||
