1xfh

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(New page: 200px<br /><applet load="1xfh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xfh, resolution 3.50&Aring;" /> '''Structure of glutama...)
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[[Image:1xfh.gif|left|200px]]<br /><applet load="1xfh" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xfh.gif|left|200px]]<br /><applet load="1xfh" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1xfh, resolution 3.50&Aring;" />
caption="1xfh, resolution 3.50&Aring;" />
'''Structure of glutamate transporter homolog from Pyrococcus horikoshii'''<br />
'''Structure of glutamate transporter homolog from Pyrococcus horikoshii'''<br />
==Overview==
==Overview==
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Glutamate transporters are integral membrane proteins that catalyse the, concentrative uptake of glutamate from the synapse to intracellular spaces, by harnessing pre-existing ion gradients. In the central nervous system, glutamate transporters are essential for normal development and function, and are implicated in stroke, epilepsy and neurodegenerative diseases., Here we present the crystal structure of a eukaryotic glutamate, transporter homologue from Pyrococcus horikoshii. The transporter is a, bowl-shaped trimer with a solvent-filled extracellular basin extending, halfway across the membrane bilayer. At the bottom of the basin are three, independent binding sites, each cradled by two helical hairpins, reaching, from opposite sides of the membrane. We propose that transport of, glutamate is achieved by movements of the hairpins that allow alternating, access to either side of the membrane.
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Glutamate transporters are integral membrane proteins that catalyse the concentrative uptake of glutamate from the synapse to intracellular spaces by harnessing pre-existing ion gradients. In the central nervous system glutamate transporters are essential for normal development and function, and are implicated in stroke, epilepsy and neurodegenerative diseases. Here we present the crystal structure of a eukaryotic glutamate transporter homologue from Pyrococcus horikoshii. The transporter is a bowl-shaped trimer with a solvent-filled extracellular basin extending halfway across the membrane bilayer. At the bottom of the basin are three independent binding sites, each cradled by two helical hairpins, reaching from opposite sides of the membrane. We propose that transport of glutamate is achieved by movements of the hairpins that allow alternating access to either side of the membrane.
==About this Structure==
==About this Structure==
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1XFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii_ot3 Pyrococcus horikoshii ot3]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XFH OCA].
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1XFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii_ot3 Pyrococcus horikoshii ot3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFH OCA].
==Reference==
==Reference==
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[[Category: trimeric helical transmembrane protein]]
[[Category: trimeric helical transmembrane protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:03:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:12 2008''

Revision as of 13:54, 21 February 2008


1xfh, resolution 3.50Å

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Structure of glutamate transporter homolog from Pyrococcus horikoshii

Overview

Glutamate transporters are integral membrane proteins that catalyse the concentrative uptake of glutamate from the synapse to intracellular spaces by harnessing pre-existing ion gradients. In the central nervous system glutamate transporters are essential for normal development and function, and are implicated in stroke, epilepsy and neurodegenerative diseases. Here we present the crystal structure of a eukaryotic glutamate transporter homologue from Pyrococcus horikoshii. The transporter is a bowl-shaped trimer with a solvent-filled extracellular basin extending halfway across the membrane bilayer. At the bottom of the basin are three independent binding sites, each cradled by two helical hairpins, reaching from opposite sides of the membrane. We propose that transport of glutamate is achieved by movements of the hairpins that allow alternating access to either side of the membrane.

About this Structure

1XFH is a Single protein structure of sequence from Pyrococcus horikoshii ot3. Full crystallographic information is available from OCA.

Reference

Structure of a glutamate transporter homologue from Pyrococcus horikoshii., Yernool D, Boudker O, Jin Y, Gouaux E, Nature. 2004 Oct 14;431(7010):811-8. PMID:15483603

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