1zdm

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[[Image:1zdm.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of Activated CheY Bound to Xe==
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|PDB= 1zdm |SIZE=350|CAPTION= <scene name='initialview01'>1zdm</scene>, resolution 2.4&Aring;
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<StructureSection load='1zdm' size='340' side='right'caption='[[1zdm]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=XE:XENON'>XE</scene>
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<table><tr><td colspan='2'>[[1zdm]] 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=1ZDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZDM FirstGlance]. <br>
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|ACTIVITY=
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</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>
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|GENE= cheY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zdm OCA], [https://pdbe.org/1zdm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zdm RCSB], [https://www.ebi.ac.uk/pdbsum/1zdm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zdm ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1fqw|1FQW]], [[1f4v|1F4V]], [[1djm|1DJM]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zdm OCA], [http://www.ebi.ac.uk/pdbsum/1zdm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zdm RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CHEY_ECOLI CHEY_ECOLI] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and the flagellar stator.<ref>PMID:20346719</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zd/1zdm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1zdm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The chemical shift of the (129)Xe NMR signal has been shown to be extremely sensitive to the local environment around the atom and has been used to follow processes such as ligand binding by bacterial periplasmic binding proteins. Here we show that the (129)Xe shift can sense more subtle changes: magnesium binding, BeF(3)(-) activation, and peptide binding by the Escherichia coli chemotaxis Y protein. (1)H-(15)N correlation spectroscopy and X-ray crystallography were used to identify two xenon-binding cavities in CheY that are primarily responsible for the shift changes. One site is near the active site, and the other is near the peptide binding site.
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'''Crystal Structure of Activated CheY Bound to Xe'''
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Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR.,Lowery TJ, Doucleff M, Ruiz EJ, Rubin SM, Pines A, Wemmer DE Protein Sci. 2005 Apr;14(4):848-55. Epub 2005 Mar 1. PMID:15741343<ref>PMID:15741343</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1zdm" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The chemical shift of the (129)Xe NMR signal has been shown to be extremely sensitive to the local environment around the atom and has been used to follow processes such as ligand binding by bacterial periplasmic binding proteins. Here we show that the (129)Xe shift can sense more subtle changes: magnesium binding, BeF(3)(-) activation, and peptide binding by the Escherichia coli chemotaxis Y protein. (1)H-(15)N correlation spectroscopy and X-ray crystallography were used to identify two xenon-binding cavities in CheY that are primarily responsible for the shift changes. One site is near the active site, and the other is near the peptide binding site.
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*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1ZDM is a [[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=1ZDM OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR., Lowery TJ, Doucleff M, Ruiz EJ, Rubin SM, Pines A, Wemmer DE, Protein Sci. 2005 Apr;14(4):848-55. Epub 2005 Mar 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15741343 15741343]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Doucleff, M.]]
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[[Category: Doucleff M]]
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[[Category: Lowery, T J.]]
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[[Category: Lowery TJ]]
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[[Category: Pines, A.]]
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[[Category: Pines A]]
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[[Category: Rubin, S M.]]
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[[Category: Rubin SM]]
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[[Category: Ruiz, E J.]]
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[[Category: Ruiz EJ]]
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[[Category: Wemmer, D E.]]
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[[Category: Wemmer DE]]
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[[Category: activated chey]]
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[[Category: bef3]]
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[[Category: protein cavity]]
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[[Category: protein conformation assay]]
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[[Category: response regulator]]
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[[Category: xenon binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:34:32 2008''
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Current revision

Crystal Structure of Activated CheY Bound to Xe

PDB ID 1zdm

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