This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2a46

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2a46.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2a46.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2a46| PDB=2a46 | SCENE= }}
{{STRUCTURE_2a46| PDB=2a46 | SCENE= }}
-
'''Crystal structures of amFP486, a cyan fluorescent protein from Anemonia majano, and variants'''
+
===Crystal structures of amFP486, a cyan fluorescent protein from Anemonia majano, and variants===
-
==Overview==
+
<!--
-
Fluorescent proteins isolated from coral reef organisms can be roughly grouped into four color classes by emission, cyan, green, yellow, and red. To gain insight into the structural basis for cyan emission, the crystal structure of amFP486 (lambda(em)max = 486 nm) was determined by molecular replacement, and the model was refined at 1.65-A resolution. The electron density map reveals a chromophore formed from the tripeptide sequence -K-Y-G- that is indistinguishable from that of GFP (lambda(em)max = 509 nm). However, the chromophore environment closely parallels those of the yellow- and red-shifted homologs zFP538, DsRed, and eqFP611. Mutagenesis was performed for Glu-150, Ala-165, His-199, and Glu-217, which are immediately adjacent to the chromophore. His-199 and Ala-165 are key side chains responsible for the blue shift, presumably by localizing chromophore charge density on the phenolate moiety. Furthermore, in the H199T mutant the fluorescence quantum yield is reduced by a factor of approximately 110. The crystal structures of H199T (lambda(em)max = 515 nm) and E150Q (lambda(em)max = 506 nm) were determined. Remarkably, the H199T structure reveals that the stacking interaction of His-199 with the chromophore also controls the fluorescence efficiency, because the chromophore is statistically distributed in a 1:1 ratio between cis (fluorescent) and trans (nonfluorescent) conformations.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16120682}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16120682 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16120682}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Remington, S J.]]
[[Category: Remington, S J.]]
[[Category: Beta barrel]]
[[Category: Beta barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:34:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:55:32 2008''

Revision as of 10:55, 27 July 2008

Image:2a46.png

Template:STRUCTURE 2a46

Crystal structures of amFP486, a cyan fluorescent protein from Anemonia majano, and variants

Template:ABSTRACT PUBMED 16120682

About this Structure

2A46 is a Single protein structure of sequence from Anemonia majano. Full crystallographic information is available from OCA.

Reference

Crystal structures and mutational analysis of amFP486, a cyan fluorescent protein from Anemonia majano., Henderson JN, Remington SJ, Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12712-7. Epub 2005 Aug 24. PMID:16120682

Page seeded by OCA on Sun Jul 27 13:55:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a46"
Personal tools