This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1fx0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fx0.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fx0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fx0| PDB=1fx0 | SCENE= }}
{{STRUCTURE_1fx0| PDB=1fx0 | SCENE= }}
-
'''Crystal structure of the chloroplast F1-ATPase from spinach'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11032839}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11032839 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11032839}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Potential tentoxin binding site]]
[[Category: Potential tentoxin binding site]]
[[Category: Thermal stability]]
[[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 Tue Jul 1 04:04:22 2008''

Revision as of 01:04, 1 July 2008

Image:1fx0.png

Template:STRUCTURE 1fx0

Crystal structure of the chloroplast F1-ATPase from spinach

Template:ABSTRACT PUBMED 11032839

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 Tue Jul 1 04:04:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fx0"
Personal tools