2a65

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(New page: 200px<br /><applet load="2a65" size="350" color="white" frame="true" align="right" spinBox="true" caption="2a65, resolution 1.650&Aring;" /> '''Crystal structure o...)
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==Overview==
==Overview==
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Na+/Cl--dependent transporters terminate synaptic transmission by using, electrochemical gradients to drive the uptake of neurotransmitters, including the biogenic amines, from the synapse to the cytoplasm of, neurons and glia. These transporters are the targets of therapeutic and, illicit compounds, and their dysfunction has been implicated in multiple, diseases of the nervous system. Here we present the crystal structure of a, bacterial homologue of these transporters from Aquifex aeolicus, in, complex with its substrate, leucine, and two sodium ions. The protein core, consists of the first ten of twelve transmembrane segments, with segments, 1-5 related to 6-10 by a pseudo-two-fold axis in the membrane plane., Leucine and the sodium ions are bound within the protein core, halfway, across the membrane bilayer, in an occluded site devoid of water. The, leucine and ion binding sites are defined by partially unwound, transmembrane helices, with main-chain atoms and helix dipoles having key, roles in substrate and ion binding. The structure reveals the architecture, of this important class of transporter, illuminates the determinants of, substrate binding and ion selectivity, and defines the external and, internal gates.
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Na+/Cl--dependent transporters terminate synaptic transmission by using electrochemical gradients to drive the uptake of neurotransmitters, including the biogenic amines, from the synapse to the cytoplasm of neurons and glia. These transporters are the targets of therapeutic and illicit compounds, and their dysfunction has been implicated in multiple diseases of the nervous system. Here we present the crystal structure of a bacterial homologue of these transporters from Aquifex aeolicus, in complex with its substrate, leucine, and two sodium ions. The protein core consists of the first ten of twelve transmembrane segments, with segments 1-5 related to 6-10 by a pseudo-two-fold axis in the membrane plane. Leucine and the sodium ions are bound within the protein core, halfway across the membrane bilayer, in an occluded site devoid of water. The leucine and ion binding sites are defined by partially unwound transmembrane helices, with main-chain atoms and helix dipoles having key roles in substrate and ion binding. The structure reveals the architecture of this important class of transporter, illuminates the determinants of substrate binding and ion selectivity, and defines the external and internal gates.
==About this Structure==
==About this Structure==
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[[Category: Jin, Y.]]
[[Category: Jin, Y.]]
[[Category: Kawate, T.]]
[[Category: Kawate, T.]]
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[[Category: Singh, S.K.]]
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[[Category: Singh, S K.]]
[[Category: Yamashita, A.]]
[[Category: Yamashita, A.]]
[[Category: BOG]]
[[Category: BOG]]
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[[Category: membrane protein]]
[[Category: membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:55:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:02 2008''

Revision as of 14:24, 21 February 2008

Image:2a65.gif

2a65, resolution 1.650Å

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Crystal structure of LEUTAA, a bacterial homolog of Na+/Cl--dependent neurotransmitter transporters

Overview

Na+/Cl--dependent transporters terminate synaptic transmission by using electrochemical gradients to drive the uptake of neurotransmitters, including the biogenic amines, from the synapse to the cytoplasm of neurons and glia. These transporters are the targets of therapeutic and illicit compounds, and their dysfunction has been implicated in multiple diseases of the nervous system. Here we present the crystal structure of a bacterial homologue of these transporters from Aquifex aeolicus, in complex with its substrate, leucine, and two sodium ions. The protein core consists of the first ten of twelve transmembrane segments, with segments 1-5 related to 6-10 by a pseudo-two-fold axis in the membrane plane. Leucine and the sodium ions are bound within the protein core, halfway across the membrane bilayer, in an occluded site devoid of water. The leucine and ion binding sites are defined by partially unwound transmembrane helices, with main-chain atoms and helix dipoles having key roles in substrate and ion binding. The structure reveals the architecture of this important class of transporter, illuminates the determinants of substrate binding and ion selectivity, and defines the external and internal gates.

About this Structure

2A65 is a Single protein structure of sequence from Aquifex aeolicus vf5 with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters., Yamashita A, Singh SK, Kawate T, Jin Y, Gouaux E, Nature. 2005 Sep 8;437(7056):215-23. Epub 2005 Jul 24. PMID:16041361

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