5JJJ

Structure of the SRII/HtrII Complex in P64 space group ("U" shape)

Summary for 5JJJ

• Entry DOI: 10.2210/pdb5jjj/pdb
• Descriptor: Sensory rhodopsin-2, Sensory rhodopsin II transducer, RETINAL, ... (5 entities in total)
• Functional Keywords: sensory rhodopsin ii, transducer, membrane protein complex, signaling protein
• Biological source: Natronomonas pharaonis (Natronobacterium pharaonis); More
• Cellular location: Cell membrane ; Multi-pass membrane protein : P42196 P42259
• Total number of polymer chains: 2
• Total formula weight: 43844.44

Authors

Ishchenko, A.,Round, E.,Borshchevskiy, V.,Grudinin, S.,Gushchin, I.,Klare, J.,Remeeva, A.,Polovinkin, V.,Utrobin, P.,Balandin, T.,Engelhard, M.,Bueldt, G.,Gordeliy, V. (deposition date: 2016-04-24, release date: 2017-02-15, Last modification date: 2024-01-10)

Primary citation

Ishchenko, A.,Round, E.,Borshchevskiy, V.,Grudinin, S.,Gushchin, I.,Klare, J.P.,Remeeva, A.,Polovinkin, V.,Utrobin, P.,Balandin, T.,Engelhard, M.,Buldt, G.,Gordeliy, V.
New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex.
Sci Rep, 7:41811-41811, 2017

PubMed Abstract: The complex of two membrane proteins, sensory rhodopsin II (NpSRII) with its cognate transducer (NpHtrII), mediates negative phototaxis in halobacteria N. pharaonis. Upon light activation NpSRII triggers a signal transduction chain homologous to the two-component system in eubacterial chemotaxis. Here we report on crystal structures of the ground and active M-state of the complex in the space group I222. We demonstrate that the relative orientation of symmetrical parts of the dimer is parallel ("U"-shaped) contrary to the gusset-like ("V"-shaped) form of the previously reported structures of the NpSRII/NpHtrII complex in the space group P222, although the structures of the monomers taken individually are nearly the same. Computer modeling of the HAMP domain in the obtained "V"- and "U"-shaped structures revealed that only the "U"-shaped conformation allows for tight interactions of the receptor with the HAMP domain. This is in line with existing data and supports biological relevance of the "U" shape in the ground state. We suggest that the "V"-shaped structure may correspond to the active state of the complex and transition from the "U" to the "V"-shape of the receptor-transducer complex can be involved in signal transduction from the receptor to the signaling domain of NpHtrII.

PubMed: 28165484
DOI: 10.1038/srep41811

Experimental method

X-RAY DIFFRACTION (2.5 Å)