1f6g: Difference between revisions

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-[[Image:1f6g.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1f6g", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1f6g|  PDB=1f6g  |  SCENE=  }}
-'''POTASSIUM CHANNEL (KCSA) FULL-LENGTH FOLD'''
+==POTASSIUM CHANNEL (KCSA) FULL-LENGTH FOLD==
+<StructureSection load='1f6g' size='340' side='right'caption='[[1f6g]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1f6g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. The February 2003 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Potassium Channels''  by Shuchismita Dutta and David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2003_2 10.2210/rcsb_pdb/mom_2003_2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F6G FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1f6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6g OCA], [https://pdbe.org/1f6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f6g RCSB], [https://www.ebi.ac.uk/pdbsum/1f6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f6g ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/KCSA_STRLI KCSA_STRLI] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).<ref>PMID:7489706</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/1f6g_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1f6g ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The molecular architecture of the NH(2) and COOH termini of the prokaryotic potassium channel KcsA has been determined using site-directed spin-labeling methods and paramagnetic resonance EPR spectroscopy. Cysteine mutants were generated (residues 5-24 and 121-160) and spin labeled, and the X-band CW EPR spectra were obtained from liposome-reconstituted channels at room temperature. Data on probe mobility (DeltaHo(-1)), accessibility parameters (PiO(2) and PiNiEdda), and inter-subunit spin-spin interaction (Omega) were used as structural constraints to build a three-dimensional folding model of these cytoplasmic domains from a set of simulated annealing and restrained molecular dynamics runs. 32 backbone structures were generated and averaged using fourfold symmetry, and a final mean structure was obtained from the eight lowest energy runs. Based on the present data, together with information from the KcsA crystal structure, a model for the three-dimensional fold of full-length KcsA was constructed. In this model, the NH(2) terminus of KcsA forms an alpha-helix anchored at the membrane-water interface, while the COOH terminus forms a right-handed four-helix bundle that extend some 40-50 A towards the cytoplasm. Functional analysis of COOH-terminal deletion constructs suggest that, while the COOH terminus does not play a substantial role in determining ion permeation properties, it exerts a modulatory role in the pH-dependent gating mechanism.
-==Overview==
+Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating.,Cortes DM, Cuello LG, Perozo E J Gen Physiol. 2001 Feb;117(2):165-80. PMID:11158168<ref>PMID:11158168</ref>
-The molecular architecture of the NH(2) and COOH termini of the prokaryotic potassium channel KcsA has been determined using site-directed spin-labeling methods and paramagnetic resonance EPR spectroscopy. Cysteine mutants were generated (residues 5-24 and 121-160) and spin labeled, and the X-band CW EPR spectra were obtained from liposome-reconstituted channels at room temperature. Data on probe mobility (DeltaHo(-1)), accessibility parameters (PiO(2) and PiNiEdda), and inter-subunit spin-spin interaction (Omega) were used as structural constraints to build a three-dimensional folding model of these cytoplasmic domains from a set of simulated annealing and restrained molecular dynamics runs. 32 backbone structures were generated and averaged using fourfold symmetry, and a final mean structure was obtained from the eight lowest energy runs. Based on the present data, together with information from the KcsA crystal structure, a model for the three-dimensional fold of full-length KcsA was constructed. In this model, the NH(2) terminus of KcsA forms an alpha-helix anchored at the membrane-water interface, while the COOH terminus forms a right-handed four-helix bundle that extend some 40-50 A towards the cytoplasm. Functional analysis of COOH-terminal deletion constructs suggest that, while the COOH terminus does not play a substantial role in determining ion permeation properties, it exerts a modulatory role in the pH-dependent gating mechanism.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-F6G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. The following page contains interesting information on the relation of 1F6G with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb38_1.html Potassium Channels]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6G OCA].
+</div>
+<div class="pdbe-citations 1f6g" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating., Cortes DM, Cuello LG, Perozo E, J Gen Physiol. 2001 Feb;117(2):165-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11158168 11158168]
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Potassium Channels]]
-[[Category: Single protein]]
+[[Category: RCSB PDB Molecule of the Month]]
 [[Category: Streptomyces lividans]]
-[[Category: Cortes, D M.]]
+[[Category: Cortes DM]]
-[[Category: Perozo, E.]]
+[[Category: Perozo E]]
-[[Category: Cytoplasmic domain]]
-[[Category: Integral membrane protein]]
-[[Category: Potassium channel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:57:36 2008''