We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2o2b

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2o2b.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2o2b.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2o2b| PDB=2o2b | SCENE= }}
{{STRUCTURE_2o2b| PDB=2o2b | SCENE= }}
-
'''Spectroscopic and Structural Study of the Heterotropic Linkage between Halide and Proton Ion Binding to Gfp Proteins: E2(GFP)-I Complex'''
+
===Spectroscopic and Structural Study of the Heterotropic Linkage between Halide and Proton Ion Binding to Gfp Proteins: E2(GFP)-I Complex===
-
==Overview==
+
<!--
-
This study reports the influence of halogens on fluorescence properties of the Aequorea victoria Green Fluorescent Protein variant S65T/T203Y (E(2)GFP). Halide binding forms a specific nonfluorescent complex generating a substantial drop of the fluorescence via static quenching. Spectroscopic analysis under different solution conditions reveals high halogen affinity, which is strongly dependent on the pH. This evidences the presence in E(2)GFP of interacting binding sites for halide ions and for protons. Thermodynamic link and cooperative interaction are assessed demonstrating that binding of one halide ion is associated with the binding of one proton in a cooperative fashion with the formation, in the pH range 4.5-10, of a single fully protonated E(2)GFP.halogen complex. To resolve the structural determinants of E(2)GFP sensitivity to halogens, high-resolution crystallographic structures were obtained for the halide-free and I(-), Br(-), and Cl(-) bound E(2)GFP. Remarkably the first high-resolution (1.4 A) crystallographic structure of a chloride-bound GFP is reported. The chloride ion occupies a specific and unique binding pocket in direct contact (3.4 A) with the chromophore imidazolidinone aromatic ring. Unanticipated flexibility, strongly modulated by halide ion interactions, is observed in the region surrounding the chromophore. Furthermore molecular dynamics simulations identified E222 residue (along with the chromophore Y66 residue) being in the protonated state when E(2)GFP.halogen complex is formed. The impact of these results on high-sensitivity biosensor design will be discussed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17434942}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17434942 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17434942}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Photoactive protein]]
[[Category: Photoactive protein]]
[[Category: Variant]]
[[Category: Variant]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:13:50 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:48:25 2008''

Revision as of 06:48, 29 July 2008

Image:2o2b.png

Template:STRUCTURE 2o2b

Spectroscopic and Structural Study of the Heterotropic Linkage between Halide and Proton Ion Binding to Gfp Proteins: E2(GFP)-I Complex

Template:ABSTRACT PUBMED 17434942

About this Structure

2O2B is a Single protein structure of sequence from Aequorea victoria. Full crystallographic information is available from OCA.

Reference

Spectroscopic and structural study of proton and halide ion cooperative binding to gfp., Arosio D, Garau G, Ricci F, Marchetti L, Bizzarri R, Nifosi R, Beltram F, Biophys J. 2007 Jul 1;93(1):232-44. Epub 2007 Apr 13. PMID:17434942

Page seeded by OCA on Tue Jul 29 09:48:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o2b"
Personal tools