1fx0
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1fx0.gif|left|200px]] | [[Image:1fx0.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1fx0", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_1fx0| PDB=1fx0 | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''Crystal structure of the chloroplast F1-ATPase from spinach''' | '''Crystal structure of the chloroplast F1-ATPase from spinach''' | ||
Line 23: | Line 20: | ||
==Reference== | ==Reference== | ||
The structure of the chloroplast F1-ATPase at 3.2 A resolution., Groth G, Pohl E, J Biol Chem. 2001 Jan 12;276(2):1345-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11032839 11032839] | The structure of the chloroplast F1-ATPase at 3.2 A resolution., Groth G, Pohl E, J Biol Chem. 2001 Jan 12;276(2):1345-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11032839 11032839] | ||
- | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Spinacia oleracea]] | [[Category: Spinacia oleracea]] | ||
[[Category: Groth, G.]] | [[Category: Groth, G.]] | ||
[[Category: Pohl, E.]] | [[Category: Pohl, E.]] | ||
- | [[Category: | + | [[Category: Latent atpase]] |
- | [[Category: | + | [[Category: Potential tentoxin binding site]] |
- | [[Category: | + | [[Category: Thermal stability]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:51:39 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 13:51, 2 May 2008
Crystal structure of the chloroplast F1-ATPase from spinach
Overview
The structure of the F(1)-ATPase from spinach chloroplasts was determined to 3.2 A resolution by molecular replacement based on the homologous structure of the bovine mitochondrial enzyme. The crystallized complex contains four different subunits in a stoichiometry of alpha(3)beta(3)gammaepsilon. Subunit delta was removed before crystallization to improve the diffraction of the crystals. The overall structure of the noncatalytic alpha-subunits and the catalytic beta-subunits is highly similar to those of the mitochondrial and thermophilic subunits. However, in the crystal structure of the chloroplast enzyme, all alpha- and beta-subunits adopt a closed conformation and appear to contain no bound adenine nucleotides. The superimposed crystallographic symmetry in the space group R32 impaired an exact tracing of the gamma- and epsilon-subunits in the complex. However, clear electron density was present at the core of the alpha(3)beta(3)-subcomplex, which probably represents the C-terminal domain of the gamma-subunit. The structure of the spinach chloroplast F(1) has a potential binding site for the phytotoxin, tentoxin, at the alphabeta-interface near betaAsp(83) and an insertion from betaGly(56)-Asn(60) in the N-terminal beta-barrel domain probably increases the thermal stability of the complex. The structure probably represents an inactive latent state of the ATPase, which is unique to chloroplast and cyanobacterial enzymes.
About this Structure
1FX0 is a Protein complex structure of sequences from Spinacia oleracea. Full crystallographic information is available from OCA.
Reference
The structure of the chloroplast F1-ATPase at 3.2 A resolution., Groth G, Pohl E, J Biol Chem. 2001 Jan 12;276(2):1345-52. PMID:11032839 Page seeded by OCA on Fri May 2 16:51:39 2008