4gyc: Difference between revisions
No edit summary |
No edit summary |
||
Line 10: | Line 10: | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/BACS2_NATPH BACS2_NATPH] Involved in the control of phototaxis. Seems to activate a methyl-accepting protein (HTR-II). Photoreceptor for blue light. | [https://www.uniprot.org/uniprot/BACS2_NATPH BACS2_NATPH] Involved in the control of phototaxis. Seems to activate a methyl-accepting protein (HTR-II). Photoreceptor for blue light. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer.,Ishchenko A, Round E, Borshchevskiy V, Grudinin S, Gushchin I, Klare JP, Balandin T, Remeeva A, Engelhard M, Buldt G, Gordeliy V J Photochem Photobiol B. 2013 Jun 5;123:55-8. doi:, 10.1016/j.jphotobiol.2013.03.008. Epub 2013 Mar 29. PMID:23619282<ref>PMID:23619282</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4gyc" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]] | *[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]] | ||
*[[Rhodopsin 3D structures|Rhodopsin 3D structures]] | *[[Rhodopsin 3D structures|Rhodopsin 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Latest revision as of 05:57, 21 November 2024
Structure of the SRII(D75N mutant)/HtrII Complex in I212121 space group ("U" shape)Structure of the SRII(D75N mutant)/HtrII Complex in I212121 space group ("U" shape)
Structural highlights
FunctionBACS2_NATPH Involved in the control of phototaxis. Seems to activate a methyl-accepting protein (HTR-II). Photoreceptor for blue light. Publication Abstract from PubMedThe 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. Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer.,Ishchenko A, Round E, Borshchevskiy V, Grudinin S, Gushchin I, Klare JP, Balandin T, Remeeva A, Engelhard M, Buldt G, Gordeliy V J Photochem Photobiol B. 2013 Jun 5;123:55-8. doi:, 10.1016/j.jphotobiol.2013.03.008. Epub 2013 Mar 29. PMID:23619282[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|