2x31

From Proteopedia

(Difference between revisions)

Revision as of 17:06, 10 April 2020

Modelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang

2x31, resolution 7.50Å

Structural highlights

2x31 is a 12 chain structure with sequence from "rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1g8p
Activity:	Magnesium chelatase, with EC number 6.6.1.1
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BCHD_RHOCB] Involved in bacteriochlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. [BCHI_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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x31"

@@ Line 3: / Line 3: @@
 <SX load='2x31' size='340' side='right' viewer='molstar' 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]. 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 [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://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>
 <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'>[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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
 == Function ==

2x31

From Proteopedia

Revision as of 17:06, 10 April 2020

Modelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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