2iia: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:2iia.jpg|left|200px]]
{{Seed}}
[[Image:2iia.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2iia|  PDB=2iia  |  SCENE=  }}  
{{STRUCTURE_2iia|  PDB=2iia  |  SCENE=  }}  


'''Anabaena sensory rhodopsin transducer'''
===Anabaena sensory rhodopsin transducer===




==Overview==
<!--
We present crystal structures of the Anabaena sensory rhodopsin transducer (ASRT), a soluble cytoplasmic protein that interacts with the first structurally characterized eubacterial retinylidene photoreceptor Anabaena sensory rhodopsin (ASR). Four crystal structures of ASRT from three different spacegroups were obtained, in all of which ASRT is present as a planar (C4) tetramer, consistent with our characterization of ASRT as a tetramer in solution. The ASRT tetramer is tightly packed, with large interfaces where the well-structured beta-sandwich portion of the monomers provides the bulk of the tetramer-forming interactions, and forms a flat, stable surface on one side of the tetramer (the beta-face). Only one of our four different ASRT crystals reveals a C-terminal alpha-helix in the otherwise all-beta protein, together with a large loop from each monomer on the opposite face of the tetramer (the alpha-face), which is flexible and largely disordered in the other three crystal forms. Gel-filtration chromatography demonstrated that ASRT forms stable tetramers in solution and isothermal microcalorimetry showed that the ASRT tetramer binds to ASR with a stoichiometry of one ASRT tetramer per one ASR photoreceptor with a K(d) of 8 microM in the highest affinity measurements. Possible mechanisms for the interaction of this transducer tetramer with the ASR photoreceptor via its flexible alpha-face to mediate transduction of the light signal are discussed.
The line below this paragraph, {{ABSTRACT_PUBMED_17289074}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17289074 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17289074}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Rhodopsin]]
[[Category: Rhodopsin]]
[[Category: Transducer]]
[[Category: Transducer]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:32:24 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:40:52 2008''

Revision as of 14:40, 27 July 2008

File:2iia.png

Template:STRUCTURE 2iia

Anabaena sensory rhodopsin transducer

Template:ABSTRACT PUBMED 17289074

About this Structure

2IIA is a Single protein structure of sequence from Anabaena sp.. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Anabaena sensory rhodopsin transducer., Vogeley L, Trivedi VD, Sineshchekov OA, Spudich EN, Spudich JL, Luecke H, J Mol Biol. 2007 Mar 30;367(3):741-51. Epub 2006 Dec 1. PMID:17289074

Page seeded by OCA on Sun Jul 27 17:40:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2iia&oldid=658755"