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| | ==Structure of TM1_TM2 in LPPG micelles== | | ==Structure of TM1_TM2 in LPPG micelles== |
| - | <StructureSection load='2k9p' size='340' side='right' caption='[[2k9p]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2k9p' size='340' side='right'caption='[[2k9p]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2k9p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K9P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K9P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2k9p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K9P FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STE2, YFL026W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9p OCA], [http://pdbe.org/2k9p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k9p RCSB], [http://www.ebi.ac.uk/pdbsum/2k9p PDBsum]</span></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=2k9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9p OCA], [https://pdbe.org/2k9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k9p RCSB], [https://www.ebi.ac.uk/pdbsum/2k9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k9p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/STE2_YEAST STE2_YEAST]] Receptor for the peptide pheromone alpha factor, the mating factor of yeast. | + | [https://www.uniprot.org/uniprot/STE2_YEAST STE2_YEAST] Receptor for the peptide pheromone alpha factor, the mating factor of yeast. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/2k9p_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/2k9p_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Naider, F]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Neumoin, N]] | + | [[Category: Naider F]] |
| - | [[Category: Zerbe, O]] | + | [[Category: Neumoin N]] |
| - | [[Category: Fragment]] | + | [[Category: Zerbe O]] |
| - | [[Category: G-protein coupled receptor]]
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| - | [[Category: Glycoprotein]]
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| - | [[Category: Gpcr]]
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| - | [[Category: Membrane]]
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| - | [[Category: Membrane protein]]
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| - | [[Category: Micelle]]
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| - | [[Category: Pheromone response]]
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| - | [[Category: Phosphoprotein]]
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| - | [[Category: Receptor]]
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| - | [[Category: Structurral biology]]
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| - | [[Category: Transducer]]
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| - | [[Category: Transmembrane]]
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| Structural highlights
Function
STE2_YEAST Receptor for the peptide pheromone alpha factor, the mating factor of yeast.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure and dynamic properties of an 80-residue fragment of Ste2p, the G-protein-coupled receptor for alpha-factor of Saccharomyces cerevisiae, was studied in LPPG micelles with the use of solution NMR spectroscopy. The fragment Ste2p(G31-T110) (TM1-TM2) consisted of 19 residues from the N-terminal domain, the first TM helix (TM1), the first cytoplasmic loop, the second TM helix (TM2), and seven residues from the first extracellular loop. Multidimensional NMR experiments on [(15)N], [(15)N, (13)C], [(15)N, (13)C, (2)H]-labeled TM1-TM2 and on protein fragments selectively labeled at specific amino acid residues or protonated at selected methyl groups resulted in >95% assignment of backbone and side-chain nuclei. The NMR investigation revealed the secondary structure of specific residues of TM1-TM2. TALOS constraints and NOE connectivities were used to calculate a structure for TM1-TM2 that was highlighted by the presence of three alpha-helices encompassing residues 39-47, 49-72, and 80-103, with higher flexibility around the internal Arg(58) site of TM1. RMSD values of individually superimposed helical segments 39-47, 49-72, and 80-103 were 0.25 +/- 0.10 A, 0.40 +/- 0.13 A, and 0.57 +/- 0.19 A, respectively. Several long-range interhelical connectivities supported the folding of TM1-TM2 into a tertiary structure typified by a crossed helix that splays apart toward the extracellular regions and contains considerable flexibility in the G(56)VRSG(60) region. (15)N-relaxation and hydrogen-deuterium exchange data support a stable fold for the TM parts of TM1-TM2, whereas the solvent-exposed segments are more flexible. The NMR structure is consistent with the results of biochemical experiments that identified the ligand-binding site within this region of the receptor.
Structure of a double transmembrane fragment of a G-protein-coupled receptor in micelles.,Neumoin A, Cohen LS, Arshava B, Tantry S, Becker JM, Zerbe O, Naider F Biophys J. 2009 Apr 22;96(8):3187-96. PMID:19383463[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Neumoin A, Cohen LS, Arshava B, Tantry S, Becker JM, Zerbe O, Naider F. Structure of a double transmembrane fragment of a G-protein-coupled receptor in micelles. Biophys J. 2009 Apr 22;96(8):3187-96. PMID:19383463 doi:10.1016/j.bpj.2009.01.012
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