2ddd: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Unique behavior of a histidine responsible for an engineered green-to-red photoconversion process== | ==Unique behavior of a histidine responsible for an engineered green-to-red photoconversion process== | ||
<StructureSection load='2ddd' size='340' side='right' caption='[[2ddd]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='2ddd' size='340' side='right'caption='[[2ddd]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ddd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Favfa Favfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DDD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DDD FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ddd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Favfa Favfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DDD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DDD FirstGlance]. <br> | ||
| Line 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Green Fluorescent Protein|Green Fluorescent Protein]] | *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 36: | Line 36: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Favfa]] | [[Category: Favfa]] | ||
[[Category: Large Structures]] | |||
[[Category: Miyawaki, A]] | [[Category: Miyawaki, A]] | ||
[[Category: Nukina, N]] | [[Category: Nukina, N]] | ||
Revision as of 10:56, 4 March 2020
Unique behavior of a histidine responsible for an engineered green-to-red photoconversion processUnique behavior of a histidine responsible for an engineered green-to-red photoconversion process
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedKikGR is a fluorescent protein engineered to display green-to-red photoconvertibility that is induced by irradiation with ultraviolet or violet light. Similar to Kaede and EosFP, two naturally occurring photoconvertible proteins, KikGR contains a His(62)-Tyr(63)-Gly(64) tripeptide sequence, which forms a green chromophore that can be photoconverted to a red one via formal beta-elimination and subsequent extension of a pi-conjugated system. Using a crystallizable variant of KikGR, we determined the structures of both the green and red state at 1.55 A resolution. The double bond between His(62)-C(alpha) and His(62)-C(beta) in the red chromophore is in a cis configuration, indicating that rotation along the His(62) C(alpha)-C(beta) bond occurs following cleavage of the His(62) N(alpha)-C(alpha) bond. This structural rearrangement provides evidence that the beta-elimination reaction governing the green-to-red photoconversion of KikGR follows an E1 (elimination, unimolecular) mechanism. The E1 mechanism in photo-induced beta-elimination reactions for green-to-red conversion of fluorescent proteins.,Tsutsui H, Shimizu H, Mizuno H, Nukina N, Furuta T, Miyawaki A Chem Biol. 2009 Nov 25;16(11):1140-7. PMID:19942137[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||