4GYC

Structure of the SRII(D75N mutant)/HtrII Complex in I212121 space group ("U" shape)

Summary for 4GYC

• Entry DOI: 10.2210/pdb4gyc/pdb
• Related: 1h2s 4GY6 4GY8 4GYA
• Descriptor: Sensory rhodopsin-2, Sensory rhodopsin II transducer, RETINAL, ... (5 entities in total)
• Functional Keywords: photoreceptor, membrane 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: 42951.98

Authors

Ishchenko, A.,Round, E.,Borshchevskiy, V.,Grudinin, S.,Gushchin, I.,Klare, J.,Remeeva, A.,Utrobin, P.,Balandin, T.,Engelhard, M.,Bueldt, G.,Gordeliy, V. (deposition date: 2012-09-05, release date: 2013-05-08, Last modification date: 2024-11-20)

Primary citation

Ishchenko, A.,Round, E.,Borshchevskiy, V.,Grudinin, S.,Gushchin, I.,Klare, J.P.,Balandin, T.,Remeeva, A.,Engelhard, M.,Buldt, G.,Gordeliy, V.
Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer.
J Photochem Photobiol B, 123C:55-58, 2013

PubMed Abstract: The complex of sensory rhodopsin II (NpSRII) with its cognate transducer (NpHtrII) mediates negative phototaxis in halobacteria Natronomonas pharaonis. Upon light activation NpSRII triggers, by means of NpHtrII, a signal transduction chain homologous to the two component system in eubacterial chemotaxis. Here we report on the crystal structure of the ground state of the mutant NpSRII-D75N/NpHtrII complex in the space group I212121. Mutations of this aspartic acid in light-driven proton pumps dramatically modify or/and inhibit protein functions. However, in vivo studies show that the similar D75N mutation retains functionality of the NpSRII/NpHtrII complex. The structure provides the molecular basis for the explanation of the unexpected observation that the wild and the mutant complexes display identical physiological response on light excitation.

PubMed: 23619282
DOI: 10.1016/j.jphotobiol.2013.03.008

Experimental method

X-RAY DIFFRACTION (2.0501 Å)