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PDBsum entry 2x31
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protein Protein-protein interface(s) links
Ligase PDB id
2x31

 

 

 

 

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Contents
Protein chains
(+ 0 more) 188 a.a. *
(+ 0 more) 322 a.a. *
* Residue conservation analysis
PDB id:
2x31
Name: Ligase
Title: Modelling of the complex between subunits bchi and bchd of magnesium chelatase based on single-particle cryo-em reconstruction at 7.5 ang
Structure: Magnesium-chelatase 60 kda subunit. Chain: a, b, c, d, e, f. Fragment: residues 373-561. Synonym: mg-protoporphyrin ix chelatase, mg-chelatase subunit d. Engineered: yes. Magnesium-chelatase 38 kda subunit. Chain: g, h, i, j, k, l. Synonym: mg-protoporphyrin ix chelatase. Engineered: yes
Source: Rhodobacter capsulatus. Organism_taxid: 1061. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Authors: J.Lunqvist,H.Elmlund,R.Peterson Wulff,L.Berglund,D.Elmlund, C.Emanuelsson,H.Hebert,R.D.Willows,M.Hansson,M.Lindahl,S.Al- Karadaghi
Key ref: J.Lundqvist et al. (2010). ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase. Structure, 18, 354-365. PubMed id: 20223218
Date:
19-Jan-10     Release date:   10-Nov-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P26175  (BCHD_RHOCB) -  Magnesium-chelatase 60 kDa subunit from Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Seq:
Struc: 		 
Seq:
Struc: 		561 a.a.
188 a.a.
Protein chains
Pfam   ArchSchema ?
P26239  (BCHI_RHOCB) -  Magnesium-chelatase 38 kDa subunit from Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Seq:
Struc: 		350 a.a.
322 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F, G, H, I, J, K, L: E.C.6.6.1.1  - magnesium chelatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		Heme and Chlorophyll Biosynthesis
      Reaction: protoporphyrin IX + Mg2+ + ATP + H2O = Mg-protoporphyrin IX + ADP + phosphate + 3 H+
protoporphyrin IX
 + Mg(2+)
 + ATP
 + H2O
 = Mg-protoporphyrin IX
 + ADP
 + phosphate
 + 3 × H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Structure 18:354-365 (2010)
PubMed id: 20223218  
 
 
ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase.
J.Lundqvist, H.Elmlund, R.P.Wulff, L.Berglund, D.Elmlund, C.Emanuelsson, H.Hebert, R.D.Willows, M.Hansson, M.Lindahl, S.Al-Karadaghi.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20955518 A.Sawicki, and R.D.Willows (2010).
BchJ and BchM interact in a 1 : 1 ratio with the magnesium chelatase BchH subunit of Rhodobacter capsulatus.
  FEBS J, 277, 4709-4721.  
20637414 D.Elmlund, R.Davis, and H.Elmlund (2010).
Ab initio structure determination from electron microscopic images of single molecules coexisting in different functional states.
  Structure, 18, 777-786.  
20223208 D.W.Bollivar (2010).
Putting metal in the middle.
  Structure, 18, 277-278.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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