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New page: left|200px<br /><applet load="2hfo" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hfo, resolution 2.10Å" /> '''Crystal Structures o...
 
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==Overview==
==Overview==
Crystal structures of the Synechocystis BLUF phototaxis photoreceptor, Slr1694 have been determined in two crystal forms, a monoclinic form at, 1.8 A resolution and an orthorhombic form at 2.1 A resolution. In both, forms, the photoreceptor is comprised of two pentamer rings stacked face, to face. Twenty total subunits in the two asymmetric units of these, crystal forms display three distinct tertiary structures that differ in, the length of the fifth beta-strand and in the orientation of Trp91, a, conserved Trp residue near the FMN chromophore. Fluorescence spectroscopic, analysis on Slr1694 in solution is consistent with motion of Trp91 from a, hydrophobic environment in the dark state to a more hydrophilic, environment in the light-excited state. Mutational analysis indicates that, movement of Trp91 is dependent on the occupancy of the hydrophobic Trp, binding pocket with a nearby Met. These different tertiary structures may, be associated with absorption changes in the blue region of the spectrum.
Crystal structures of the Synechocystis BLUF phototaxis photoreceptor Slr1694 have been determined in two crystal forms, a monoclinic form at 1.8 A resolution and an orthorhombic form at 2.1 A resolution. In both forms, the photoreceptor is comprised of two pentamer rings stacked face to face. Twenty total subunits in the two asymmetric units of these crystal forms display three distinct tertiary structures that differ in the length of the fifth beta-strand and in the orientation of Trp91, a conserved Trp residue near the FMN chromophore. Fluorescence spectroscopic analysis on Slr1694 in solution is consistent with motion of Trp91 from a hydrophobic environment in the dark state to a more hydrophilic environment in the light-excited state. Mutational analysis indicates that movement of Trp91 is dependent on the occupancy of the hydrophobic Trp binding pocket with a nearby Met. These different tertiary structures may be associated with absorption changes in the blue region of the spectrum.


==About this Structure==
==About this Structure==
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[[Category: Synechocystis sp.]]
[[Category: Synechocystis sp.]]
[[Category: Anderson, S.]]
[[Category: Anderson, S.]]
[[Category: Bauer, C.E.]]
[[Category: Bauer, C E.]]
[[Category: Dragnea, V.]]
[[Category: Dragnea, V.]]
[[Category: Masuda, S.]]
[[Category: Masuda, S.]]
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[[Category: photoreceptor]]
[[Category: photoreceptor]]


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Revision as of 15:41, 21 February 2008

File:2hfo.jpg


2hfo, resolution 2.10Å

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Crystal Structures of the Synechocystis Photoreceptor Slr1694 Reveal Distinct Structural States Related to Signaling

Overview

Crystal structures of the Synechocystis BLUF phototaxis photoreceptor Slr1694 have been determined in two crystal forms, a monoclinic form at 1.8 A resolution and an orthorhombic form at 2.1 A resolution. In both forms, the photoreceptor is comprised of two pentamer rings stacked face to face. Twenty total subunits in the two asymmetric units of these crystal forms display three distinct tertiary structures that differ in the length of the fifth beta-strand and in the orientation of Trp91, a conserved Trp residue near the FMN chromophore. Fluorescence spectroscopic analysis on Slr1694 in solution is consistent with motion of Trp91 from a hydrophobic environment in the dark state to a more hydrophilic environment in the light-excited state. Mutational analysis indicates that movement of Trp91 is dependent on the occupancy of the hydrophobic Trp binding pocket with a nearby Met. These different tertiary structures may be associated with absorption changes in the blue region of the spectrum.

About this Structure

2HFO is a Single protein structure of sequence from Synechocystis sp. with FMN as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structures of the Synechocystis photoreceptor Slr1694 reveal distinct structural states related to signaling., Yuan H, Anderson S, Masuda S, Dragnea V, Moffat K, Bauer C, Biochemistry. 2006 Oct 24;45(42):12687-94. PMID:17042486

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