Methyl-accepting chemotaxis protein: Difference between revisions

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[[Image:1xbn.png|left|200px|thumb|Crystal Structure of Methyl-accepting chemotaxis protein [[1xbn]]]]
[[Image:1xbn.png|left|200px|thumb|Crystal Structure of Methyl-accepting chemotaxis protein [[1xbn]]]]
{{STRUCTURE_1xbn|  PDB=1xbn  | SIZE=300| SCENE= |right|CAPTION=Methyl-accepting chemotaxis protein with Fe-protoporphyrin IX + O2 [[1xbn]] }}
{{STRUCTURE_1xbn|  PDB=1xbn  | SIZE=300| SCENE=Methyl-accepting_chemotaxis_protein/Cv/1 |right|CAPTION=Methyl-accepting chemotaxis protein with Fe-protoporphyrin IX + O2 [[1xbn]] }}


[[Methyl-accepting chemotaxis protein]] (MCP) are proteins of the inner cytoplasmic face of bacterial plasma membrane with which the receptors of the outer face interact.  MCP undergo reversible methylation as part of the adaptation to the signal.  MCP which are NO sensing contain a heme-NO and oxygen-binding domain (H-NOX). The images at the left and at the right correspond to one representative MCP, ''i.e.'' the crystal structure of Methyl-accepting chemotaxis protein from ''Thermoanaerobacter tengcongensis'' ([[3hbt]]).
[[Methyl-accepting chemotaxis protein]] (MCP) are proteins of the inner cytoplasmic face of bacterial plasma membrane with which the receptors of the outer face interact.  MCP undergo reversible methylation as part of the adaptation to the signal.  MCP which are NO sensing contain a heme-NO and oxygen-binding domain (H-NOX). The images at the left and at the right correspond to one representative MCP, ''i.e.'' the crystal structure of Methyl-accepting chemotaxis protein from ''Thermoanaerobacter tengcongensis'' ([[3hbt]]).

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Alexander Berchansky, Michal Harel