3atp
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3atp is ON HOLD Authors: Tajima, H., Sakuma, M., Homma, K., Kawagishi, I., Imada, K. Description: Structure of the ligand binding domain of the bac...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the ligand binding domain of the bacterial serine chemoreceptor Tsr with ligand== | |
| + | <StructureSection load='3atp' size='340' side='right'caption='[[3atp]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3atp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._W3110 Escherichia coli str. K-12 substr. W3110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ATP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ATP FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SER:SERINE'>SER</scene></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=3atp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3atp OCA], [https://pdbe.org/3atp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3atp RCSB], [https://www.ebi.ac.uk/pdbsum/3atp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3atp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MCP1_ECOLI MCP1_ECOLI] Receptor for the attractant L-serine and related amino acids. Is also responsible for chemotaxis away from a wide range of repellents, including leucine, indole, and weak acids. Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB. | ||
| - | + | ==See Also== | |
| - | + | *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli str. K-12 substr. W3110]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Homma K]] | ||
| + | [[Category: Imada K]] | ||
| + | [[Category: Kawagishi I]] | ||
| + | [[Category: Sakuma M]] | ||
| + | [[Category: Tajima H]] | ||
Current revision
Structure of the ligand binding domain of the bacterial serine chemoreceptor Tsr with ligand
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