1id1: Difference between revisions

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New page: left|200px<br /><applet load="1id1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1id1, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1id1.jpg|left|200px]]<br /><applet load="1id1" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1id1.jpg|left|200px]]<br /><applet load="1id1" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1id1, resolution 2.4&Aring;" />
caption="1id1, resolution 2.4&Aring;" />
'''CRYSTAL STRUCTURE OF THE RCK DOMAIN FROM E.COLI POTASSIUM CHANNEL'''<br />
'''CRYSTAL STRUCTURE OF THE RCK DOMAIN FROM E.COLI POTASSIUM CHANNEL'''<br />


==Overview==
==Overview==
The intracellular C-terminal domain structure of a six-transmembrane K+, channel from Escherichia coli has been solved by X-ray crystallography at, 2.4 A resolution. The structure is representative of a broad class of, domains/proteins that regulate the conductance of K+ (here referred to as, RCK domains) in prokaryotic K+ transporters and K+ channels. The RCK, domain has a Rossmann-fold topology with unique positions, not commonly, conserved among Rossmann-fold proteins, composing a well-conserved salt, bridge and a hydrophobic dimer interface. Structure-based amino acid, sequence alignments and mutational analysis are used to demonstrate that, an RCK domain is also present and is an important component of the gating, machinery in eukaryotic large-conductance Ca2+ activated K+ channels.
The intracellular C-terminal domain structure of a six-transmembrane K+ channel from Escherichia coli has been solved by X-ray crystallography at 2.4 A resolution. The structure is representative of a broad class of domains/proteins that regulate the conductance of K+ (here referred to as RCK domains) in prokaryotic K+ transporters and K+ channels. The RCK domain has a Rossmann-fold topology with unique positions, not commonly conserved among Rossmann-fold proteins, composing a well-conserved salt bridge and a hydrophobic dimer interface. Structure-based amino acid sequence alignments and mutational analysis are used to demonstrate that an RCK domain is also present and is an important component of the gating machinery in eukaryotic large-conductance Ca2+ activated K+ channels.


==About this Structure==
==About this Structure==
1ID1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ID1 OCA].  
1ID1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID1 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cadene, M.]]
[[Category: Cadene, M.]]
[[Category: Chait, B.T.]]
[[Category: Chait, B T.]]
[[Category: Jiang, Y.]]
[[Category: Jiang, Y.]]
[[Category: MacKinnon, R.]]
[[Category: MacKinnon, R.]]
[[Category: Pico, A.]]
[[Category: Pico, A.]]
[[Category: bk channel]]
[[Category: bk channel]]
[[Category: e.coli potassium channel]]
[[Category: e coli potassium channel]]
[[Category: rck domain]]
[[Category: rck domain]]
[[Category: rossmann fold]]
[[Category: rossmann fold]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:36 2008''

Revision as of 14:10, 21 February 2008

File:1id1.jpg


1id1, resolution 2.4Å

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CRYSTAL STRUCTURE OF THE RCK DOMAIN FROM E.COLI POTASSIUM CHANNEL

OverviewOverview

The intracellular C-terminal domain structure of a six-transmembrane K+ channel from Escherichia coli has been solved by X-ray crystallography at 2.4 A resolution. The structure is representative of a broad class of domains/proteins that regulate the conductance of K+ (here referred to as RCK domains) in prokaryotic K+ transporters and K+ channels. The RCK domain has a Rossmann-fold topology with unique positions, not commonly conserved among Rossmann-fold proteins, composing a well-conserved salt bridge and a hydrophobic dimer interface. Structure-based amino acid sequence alignments and mutational analysis are used to demonstrate that an RCK domain is also present and is an important component of the gating machinery in eukaryotic large-conductance Ca2+ activated K+ channels.

About this StructureAbout this Structure

1ID1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel., Jiang Y, Pico A, Cadene M, Chait BT, MacKinnon R, Neuron. 2001 Mar;29(3):593-601. PMID:11301020

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