2x31: Difference between revisions

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[[Image:2x31.png|left|200px]]
==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]] 7.50&Aring;' scene=''>
== 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]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g8p|1g8p]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
<tr><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://www.rcsb.org/pdb/explore.do?structureId=2x31 RCSB], [http://www.ebi.ac.uk/pdbsum/2x31 PDBsum]</span></td></tr>
<table>
<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.


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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>
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===Modelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
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== References ==
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[[Category: Rhodonostoc capsulatum molisch 1907]]
{{ABSTRACT_PUBMED_20223218}}
 
==About this Structure==
[[2x31]] is a 12 chain structure with sequence from [http://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].
 
==Reference==
<ref group="xtra">PMID:020223218</ref><references group="xtra"/>
[[Category: Magnesium chelatase]]
[[Category: Magnesium chelatase]]
[[Category: Rhodobacter capsulatus]]
[[Category: Al-Karadaghi, S.]]
[[Category: Al-Karadaghi, S.]]
[[Category: Berglund, L.]]
[[Category: Berglund, L.]]
Retrieved from "https://proteopedia.org/2x31"