Methyl-accepting chemotaxis protein

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PDB ID 1xbn

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Methyl-accepting chemotaxis protein with Fe-protoporphyrin IX + O2 1xbn
Ligands: ,
Gene: Tar4 (Thermoanaerobacter tengcongensis MB4)
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml

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). For more details see Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor.

3D Structures of Methyl-accepting chemotaxis protein

3g67 – TmMCP – Thermotoga maritima
3g6b - TmMCP (mutant)
2ch7 – TmMCP cytoplasmic domain
3c8c - MCP N terminal – Vibrio cholerae
2qhx - MCP N terminal – Vibrio parahaemolyticus
2d4u – EcMCP ligand-binding domain (mutant) – Eschericia coli
1qu7 - EcMCP I cytoplasmic domain
1jmw - MCP II ligand-binding domain (mutant) – Salmonella typhimurium

Heme-containing MCP

3sj5 – MCP (mutant) with Fe-protoporphyrin IX – Caldanaerobacter subterraneus
3nvr, 3nvu, 3iqb, 3eee – TtMCP N terminal (mutant) with Fe-protoporphyrin IX + O2 – Thermoanaerobacter tengcongensis
1xbn - TtMCP with Fe-protoporphyrin IX + O2
1u4h, 1u55, 1u56 - TtMCP H-NOX domain with Fe-protoporphyrin IX + O2
3lah, 3lai - TtMCP N terminal (mutant) with Fe-protoporphyrin IX + imidazole
3m0b - TtMCP N terminal with Ru-mesoporphyrin IX

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Alexander Berchansky, Michal Harel

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