From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
Line 1: |
Line 1: |
- | [[Image:1h2s.gif|left|200px]] | + | {{Seed}} |
| + | [[Image:1h2s.png|left|200px]] |
| | | |
| <!-- | | <!-- |
Line 9: |
Line 10: |
| {{STRUCTURE_1h2s| PDB=1h2s | SCENE= }} | | {{STRUCTURE_1h2s| PDB=1h2s | SCENE= }} |
| | | |
- | '''MOLECULAR BASIS OF TRANSMENBRANE SIGNALLING BY SENSORY RHODOPSIN II-TRANSDUCER COMPLEX'''
| + | ===MOLECULAR BASIS OF TRANSMENBRANE SIGNALLING BY SENSORY RHODOPSIN II-TRANSDUCER COMPLEX=== |
| | | |
| | | |
- | ==Overview==
| + | <!-- |
- | Microbial rhodopsins, which constitute a family of seven-helix membrane proteins with retinal as a prosthetic group, are distributed throughout the Bacteria, Archaea and Eukaryota. This family of photoactive proteins uses a common structural design for two distinct functions: light-driven ion transport and phototaxis. The sensors activate a signal transduction chain similar to that of the two-component system of eubacterial chemotaxis. The link between the photoreceptor and the following cytoplasmic signal cascade is formed by a transducer molecule that binds tightly and specifically to its cognate receptor by means of two transmembrane helices (TM1 and TM2). It is thought that light excitation of sensory rhodopsin II from Natronobacterium pharaonis (SRII) in complex with its transducer (HtrII) induces an outward movement of its helix F (ref. 6), which in turn triggers a rotation of TM2 (ref. 7). It is unclear how this TM2 transition is converted into a cellular signal. Here we present the X-ray structure of the complex between N. pharaonis SRII and the receptor-binding domain of HtrII at 1.94 A resolution, which provides an atomic picture of the first signal transduction step. Our results provide evidence for a common mechanism for this process in phototaxis and chemotaxis.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12368857}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 12368857 is the PubMed ID number. |
| + | --> |
| + | {{ABSTRACT_PUBMED_12368857}} |
| | | |
| ==About this Structure== | | ==About this Structure== |
Line 35: |
Line 39: |
| [[Category: Menbrane protein complex]] | | [[Category: Menbrane protein complex]] |
| [[Category: Signal transduction]] | | [[Category: Signal transduction]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:21:14 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:31:47 2008'' |
Revision as of 03:31, 1 July 2008
Template:STRUCTURE 1h2s
MOLECULAR BASIS OF TRANSMENBRANE SIGNALLING BY SENSORY RHODOPSIN II-TRANSDUCER COMPLEX
Template:ABSTRACT PUBMED 12368857
About this Structure
1H2S is a Protein complex structure of sequences from Natronomonas pharaonis. Full crystallographic information is available from OCA.
Reference
Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex., Gordeliy VI, Labahn J, Moukhametzianov R, Efremov R, Granzin J, Schlesinger R, Buldt G, Savopol T, Scheidig AJ, Klare JP, Engelhard M, Nature. 2002 Oct 3;419(6906):484-7. PMID:12368857
Page seeded by OCA on Tue Jul 1 06:31:47 2008
Categories: Natronomonas pharaonis | Protein complex | Bueldt, G. | Efremov, R. | Engelhard, M. | Gordeliy, V I. | Granzin, J. | Klare, J P. | Labahn, J. | Moukhametzianov, R. | Savopol, T. | Scheidig, A. | Schlesinger, R. | Menbrane protein complex | Signal transduction