1id1: Difference between revisions

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<StructureSection load='1id1' size='340' side='right'caption='[[1id1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1id1' size='340' side='right'caption='[[1id1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1id1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ID1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1id1]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ID1 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1id1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id1 OCA], [https://pdbe.org/1id1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1id1 RCSB], [https://www.ebi.ac.uk/pdbsum/1id1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1id1 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1id1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id1 OCA], [https://pdbe.org/1id1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1id1 RCSB], [https://www.ebi.ac.uk/pdbsum/1id1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1id1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/KCH_ECOLI KCH_ECOLI]] K(+)-specific ion channel. May play a role in the defense against osmotic shock.<ref>PMID:8170937</ref> <ref>PMID:12912904</ref>
[https://www.uniprot.org/uniprot/KCH_ECOLI KCH_ECOLI] K(+)-specific ion channel. May play a role in the defense against osmotic shock.<ref>PMID:8170937</ref> <ref>PMID:12912904</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1id1 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1id1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:11301020</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1id1" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cadene, M]]
[[Category: Cadene M]]
[[Category: Chait, B T]]
[[Category: Chait BT]]
[[Category: Jiang, Y]]
[[Category: Jiang Y]]
[[Category: MacKinnon, R]]
[[Category: MacKinnon R]]
[[Category: Pico, A]]
[[Category: Pico A]]
[[Category: Bk channel]]
[[Category: E coli potassium channel]]
[[Category: Membrane protein]]
[[Category: Rck domain]]
[[Category: Rossmann fold]]

Latest revision as of 10:34, 7 February 2024

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

Structural highlights

1id1 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KCH_ECOLI K(+)-specific ion channel. May play a role in the defense against osmotic shock.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Milkman R. An Escherichia coli homologue of eukaryotic potassium channel proteins. Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3510-4. PMID:8170937
  2. ↑ Kuo MM, Saimi Y, Kung C. Gain-of-function mutations indicate that Escherichia coli Kch forms a functional K+ conduit in vivo. EMBO J. 2003 Aug 15;22(16):4049-58. PMID:12912904 doi:http://dx.doi.org/10.1093/emboj/cdg409

1id1, resolution 2.40Å

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