Sandbox flippases

From Proteopedia

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 == Mechanism ==
-The beginning conformation is an outward-occluded conformation and the head of Linked-lipid Oligosaccharide(LLO) is on the cytoplasmic side. When the tail of LLO is attached to external helix, the ADP exchanges to ATP and the conformation changes to outward-open state. The head of LLO attaches to a positively charged belt facing to periplasmic side since the pyrophosphate has negative charge which attracts to positive charge. As ATP changes to ADP, the conformation returns to outward-occluded conformation and it squeezes the LLO head out to periplasmic side of the membrane and the tail of LLO is released to extend to cytoplasmic side. Therefore, the position of LLO is opposite through this mechanism.
+The beginning conformation is an outward-occluded conformation and the head of Linked-lipid Oligosaccharide(LLO) is on the cytoplasmic side. When the tail of LLO is attached to external helix, the ADP exchanges to ATP and the conformation changes to outward-open state. The head of LLO attaches to a positively charged belt facing to periplasmic side since the pyrophosphate has negative charge which attracts to positive charge. As ATP changes to ADP, the conformation returns to outward-occluded conformation and it squeezes the LLO head out to periplasmic side of the membrane and the tail of LLO is released to extend to cytoplasmic side. Therefore, the position of LLO is opposite through this mechanism. <ref name= "name"> Verchère, A., & Menon, A. K. (2015). Structural biology: Lipid gymnastics. Nature, 524(7566), 420-422. </ref>
 == Disease ==

Revision as of 04:34, 16 December 2015

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Flippases

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Flippases are the homodimeric transmembrane proteins located in the membrane. It helps phospholipid to transport from inner face to outer face of the cell membrane. It is composed with alpha-helix and beta sheets. The main three structural features of each monomer are an external helix, a belt of positively charged amino acids, and a binding site for an ATP molecule.

This is a default text for your page Sandbox flippases. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

1 Structural Highlights
2 Function
3 Mechanism
4 Disease
5 Relevance

Structural Highlights

The main three structural features of each monomer are an external helix, a belt of positively charged amino acids, and a binding site for an ATP molecule.

Function

Flippases flip the lipid from cytoplasmic(in) side to periplasmic(out) side.

Mechanism

The beginning conformation is an outward-occluded conformation and the head of Linked-lipid Oligosaccharide(LLO) is on the cytoplasmic side. When the tail of LLO is attached to external helix, the ADP exchanges to ATP and the conformation changes to outward-open state. The head of LLO attaches to a positively charged belt facing to periplasmic side since the pyrophosphate has negative charge which attracts to positive charge. As ATP changes to ADP, the conformation returns to outward-occluded conformation and it squeezes the LLO head out to periplasmic side of the membrane and the tail of LLO is released to extend to cytoplasmic side. Therefore, the position of LLO is opposite through this mechanism. ^[3]

Disease

Relevance

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References

↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
↑ Verchère, A., & Menon, A. K. (2015). Structural biology: Lipid gymnastics. Nature, 524(7566), 420-422.