Aconitase

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<applet load='1pw4.pdb' scene='User:Ralf_Stephan/Sandbox_1/Vertical_symm/1' size='400' frame='true' align='right' caption="GplT from E. coli is a Major Facilitator antiporter, rocker-switch type. We use it as example but the principle remains the same for all other Major Facilitators." />
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'''Major Facilitators''' are membrane proteins that help with both influx and outflux of specific small molecules. They are neither passive channels, nor do they active pumping, like the ATPases. Like a rocker-switch, they tilt between the two states 'outside open' and 'inside open'. This tilting (or switching) is triggered when a molecule has docked inside, and it transports the molecule to the other side. There are major facilitator uniporters, symporters, and antiporters. Antiporters usually transport a second, different, molecule, when switching back in the opposite direction. In 2009, there is still no structure data that would clearly show the transport process in major facilitators.
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'''Major Facilitators''' are membrane proteins that help with both influx and outflux of specific small molecules. They are neither passive channels, nor do they active pumping, like the ATPases. Like a rocker-switch, they tilt between the two states 'outside open' and 'inside open'. This tilting (or switching) is triggered when a molecule has docked inside, and it transports the molecule to the other side. We call these transporters antiporter because, when switching back, usually a second, different, molecule is transported in the opposite direction. Have a look at the complete process involving all molecules.
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[[2ns1]]
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== Classification ==
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TCDB, the most sophisticated classification of transport proteins to date, classifies the major facilitators as family 2.A.1 in the clan of '''secondary active [[porters]]'''.
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== References ==
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== Available structures ==
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<references/>
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The family has about 10,000 sequenced members from all living organisms. There are, however, only a few protein structures resolved.
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* from ''E.&nbsp;coli'' K12:
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** the [[glycerol-3-phosphate transporter]] ([[1pw4]])
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** the [[multidrug resistance protein]] D ([[2gfp]])
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** the [[lactose permease]] ([[1pv7]], [[2cfp]], [[2cfq]], [[2v8n]])
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== Weblinks ==
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*[http://www.tcdb.org/ The TCDB database]
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*[http://www.tcdb.org/tcdb/subclass2.php?tc=2.A.1 TCDB: 2.A.1 The Major Facilitator Superfamily (MFS)]
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*[http://www.tcdb.org/pdb_structure.php TCDB: Transport proteins with PDB structures]

Revision as of 16:01, 14 February 2009

Major Facilitators are membrane proteins that help with both influx and outflux of specific small molecules. They are neither passive channels, nor do they active pumping, like the ATPases. Like a rocker-switch, they tilt between the two states 'outside open' and 'inside open'. This tilting (or switching) is triggered when a molecule has docked inside, and it transports the molecule to the other side. There are major facilitator uniporters, symporters, and antiporters. Antiporters usually transport a second, different, molecule, when switching back in the opposite direction. In 2009, there is still no structure data that would clearly show the transport process in major facilitators.

Classification

TCDB, the most sophisticated classification of transport proteins to date, classifies the major facilitators as family 2.A.1 in the clan of secondary active porters.

Available structures

The family has about 10,000 sequenced members from all living organisms. There are, however, only a few protein structures resolved.

Weblinks

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