3b8c
From Proteopedia
Line 1: | Line 1: | ||
[[Image:3b8c.jpg|left|200px]] | [[Image:3b8c.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_3b8c", 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_3b8c| PDB=3b8c | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''Crystal Structure of a Plasma Membrane Proton Pump''' | '''Crystal Structure of a Plasma Membrane Proton Pump''' | ||
Line 31: | Line 28: | ||
[[Category: Palmgren, M G.]] | [[Category: Palmgren, M G.]] | ||
[[Category: Pedersen, B P.]] | [[Category: Pedersen, B P.]] | ||
- | [[Category: | + | [[Category: Acetylation]] |
- | [[Category: | + | [[Category: Atp-binding]] |
- | [[Category: | + | [[Category: Hydrogen ion transport]] |
- | [[Category: | + | [[Category: Hydrolase]] |
- | [[Category: | + | [[Category: Ion transport]] |
- | [[Category: | + | [[Category: Magnesium]] |
- | [[Category: | + | [[Category: Membrane]] |
- | [[Category: | + | [[Category: Metal-binding]] |
- | [[Category: | + | [[Category: Nucleotide-binding]] |
- | [[Category: | + | [[Category: P-type atpase]] |
- | [[Category: | + | [[Category: Phosphorylation]] |
- | [[Category: | + | [[Category: Plasma membrane]] |
- | [[Category: | + | [[Category: Proton pump]] |
- | [[Category: | + | [[Category: Transmembrane]] |
- | [[Category: | + | [[Category: Transport]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:30:49 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 17:30, 4 May 2008
Crystal Structure of a Plasma Membrane Proton Pump
Overview
A prerequisite for life is the ability to maintain electrochemical imbalances across biomembranes. In all eukaryotes the plasma membrane potential and secondary transport systems are energized by the activity of P-type ATPase membrane proteins: H+-ATPase (the proton pump) in plants and fungi, and Na+,K+-ATPase (the sodium-potassium pump) in animals. The name P-type derives from the fact that these proteins exploit a phosphorylated reaction cycle intermediate of ATP hydrolysis. The plasma membrane proton pumps belong to the type III P-type ATPase subfamily, whereas Na+,K+-ATPase and Ca2+-ATPase are type II. Electron microscopy has revealed the overall shape of proton pumps, however, an atomic structure has been lacking. Here we present the first structure of a P-type proton pump determined by X-ray crystallography. Ten transmembrane helices and three cytoplasmic domains define the functional unit of ATP-coupled proton transport across the plasma membrane, and the structure is locked in a functional state not previously observed in P-type ATPases. The transmembrane domain reveals a large cavity, which is likely to be filled with water, located near the middle of the membrane plane where it is lined by conserved hydrophilic and charged residues. Proton transport against a high membrane potential is readily explained by this structural arrangement.
About this Structure
3B8C is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
Crystal structure of the plasma membrane proton pump., Pedersen BP, Buch-Pedersen MJ, Morth JP, Palmgren MG, Nissen P, Nature. 2007 Dec 13;450(7172):1111-4. PMID:18075595 Page seeded by OCA on Sun May 4 20:30:49 2008
Categories: Arabidopsis thaliana | Proton-exporting ATPase | Single protein | Buch-Pedersen, M J. | Morth, J P. | Nissen, P. | Palmgren, M G. | Pedersen, B P. | Acetylation | Atp-binding | Hydrogen ion transport | Hydrolase | Ion transport | Magnesium | Membrane | Metal-binding | Nucleotide-binding | P-type atpase | Phosphorylation | Plasma membrane | Proton pump | Transmembrane | Transport