2x31
From Proteopedia
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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== |
+ | <StructureSection load='2x31' size='340' side='right' caption='[[2x31]], [[Resolution|resolution]] 7.50Å' 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. | ||
- | + | 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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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | < | + | <references/> |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | [[Category: Rhodonostoc capsulatum molisch 1907]] | |
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- | == | + | |
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[[Category: Magnesium chelatase]] | [[Category: Magnesium chelatase]] | ||
- | [[Category: Rhodobacter capsulatus]] | ||
[[Category: Al-Karadaghi, S.]] | [[Category: Al-Karadaghi, S.]] | ||
[[Category: Berglund, L.]] | [[Category: Berglund, L.]] |
Revision as of 07:44, 14 May 2014
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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Categories: Rhodonostoc capsulatum molisch 1907 | Magnesium chelatase | Al-Karadaghi, S. | Berglund, L. | Elmlund, D. | Elmlund, H. | Emanuelsson, C. | Hansson, M. | Hebert, H. | Lindahl, M. | Lunqvist, J. | Willows, R D. | Wulff, R Peterson. | Bacteriochlorophyll biosynthesis | Ligase | Photosynthesis