2hmt

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(New page: 200px<br /><applet load="2hmt" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hmt, resolution 2.200&Aring;" /> '''Diamond-shaped octa...)
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==Overview==
==Overview==
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The KtrAB ion transporter is a complex of the KtrB membrane protein and, KtrA, an RCK domain. RCK domains regulate eukaryotic and prokaryotic, membrane proteins involved in K(+) transport. Conflicting functional, models have proposed two different oligomeric arrangements for RCK, domains, tetramer versus octamer. Our results for the KtrAB RCK domain, clearly show an octamer in solution and in the crystal. We determined the, structure of this protein in three different octameric ring conformations, that resemble the RCK-domain octamer observed in the MthK potassium, channel but show striking differences in size and symmetry. We present, experimental evidence for the association between one RCK octameric ring, and two KtrB membrane proteins. These results provide insights into the, quaternary organization of the KtrAB transporter and its mechanism of, activation and show that the RCK-domain octameric ring model is generally, applicable to other ion-transport systems.
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The KtrAB ion transporter is a complex of the KtrB membrane protein and KtrA, an RCK domain. RCK domains regulate eukaryotic and prokaryotic membrane proteins involved in K(+) transport. Conflicting functional models have proposed two different oligomeric arrangements for RCK domains, tetramer versus octamer. Our results for the KtrAB RCK domain clearly show an octamer in solution and in the crystal. We determined the structure of this protein in three different octameric ring conformations that resemble the RCK-domain octamer observed in the MthK potassium channel but show striking differences in size and symmetry. We present experimental evidence for the association between one RCK octameric ring and two KtrB membrane proteins. These results provide insights into the quaternary organization of the KtrAB transporter and its mechanism of activation and show that the RCK-domain octameric ring model is generally applicable to other ion-transport systems.
==About this Structure==
==About this Structure==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Albright, R.A.]]
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[[Category: Albright, R A.]]
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[[Category: Morais-Cabral, J.H.]]
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[[Category: Morais-Cabral, J H.]]
[[Category: NAI]]
[[Category: NAI]]
[[Category: ion transporter]]
[[Category: ion transporter]]
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[[Category: symporter]]
[[Category: symporter]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:24:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:43:28 2008''

Revision as of 15:43, 21 February 2008


2hmt, resolution 2.200Å

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Diamond-shaped octameric ring structure of an RCK domain with NADH bound

Overview

The KtrAB ion transporter is a complex of the KtrB membrane protein and KtrA, an RCK domain. RCK domains regulate eukaryotic and prokaryotic membrane proteins involved in K(+) transport. Conflicting functional models have proposed two different oligomeric arrangements for RCK domains, tetramer versus octamer. Our results for the KtrAB RCK domain clearly show an octamer in solution and in the crystal. We determined the structure of this protein in three different octameric ring conformations that resemble the RCK-domain octamer observed in the MthK potassium channel but show striking differences in size and symmetry. We present experimental evidence for the association between one RCK octameric ring and two KtrB membrane proteins. These results provide insights into the quaternary organization of the KtrAB transporter and its mechanism of activation and show that the RCK-domain octameric ring model is generally applicable to other ion-transport systems.

About this Structure

2HMT is a Single protein structure of sequence from Bacillus subtilis with as ligand. Full crystallographic information is available from OCA.

Reference

The RCK domain of the KtrAB K+ transporter: multiple conformations of an octameric ring., Albright RA, Ibar JL, Kim CU, Gruner SM, Morais-Cabral JH, Cell. 2006 Sep 22;126(6):1147-59. PMID:16990138

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