2hmv: Difference between revisions

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==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.

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==

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[[Category: Bacillus subtilis]]

[[Category: Single protein]]

[[Category: Albright, R.A.]]

[[Category: Albright, R A.]]

[[Category: Morais-Cabral, J.H.]]

[[Category: Morais-Cabral, J H.]]

[[Category: ADP]]

[[Category: ion transporter]]

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[[Category: symporter]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:43:28 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Bacillus subtilis]]
 [[Category: Single protein]]
-[[Category: Albright, R.A.]]
+[[Category: Albright, R A.]]
-[[Category: Morais-Cabral, J.H.]]
+[[Category: Morais-Cabral, J H.]]
 [[Category: ADP]]
 [[Category: ion transporter]]
@@ Line 25: / Line 25: @@
 [[Category: symporter]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:24:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:43:28 2008''