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.


1jc1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jc1.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1jc1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jc1| PDB=1jc1 | SCENE= }}
{{STRUCTURE_1jc1| PDB=1jc1 | SCENE= }}
-
'''CRYSTAL STRUCTURE ANALYSIS OF A REDOX-SENSITIVE GREEN FLUORESCENT PROTEIN VARIANT IN A OXIDIZED FORM'''
+
===CRYSTAL STRUCTURE ANALYSIS OF A REDOX-SENSITIVE GREEN FLUORESCENT PROTEIN VARIANT IN A OXIDIZED FORM===
-
==Overview==
+
<!--
-
Current methods for determining ambient redox potential in cells are labor-intensive and generally require destruction of tissue. This precludes single cell or real time studies of changes in redox poise that result from metabolic processes or environmental influences. By substitution of surface-exposed residues on the Aequorea victoria green fluorescent protein (GFP) with cysteines in appropriate positions to form disulfide bonds, reduction-oxidation-sensitive GFPs (roGFPs) have been created. roGFPs have two fluorescence excitation maxima at about 400 and 490 nm and display rapid and reversible ratiometric changes in fluorescence in response to changes in ambient redox potential in vitro and in vivo. Crystal structure analyses of reduced and oxidized crystals of roGFP2 at 2.0- and 1.9-A resolution, respectively, reveal in the oxidized state a highly strained disulfide and localized main chain structural changes that presumably account for the state-dependent spectral changes. roGFP1 has been targeted to the mitochondria in HeLa cells. Fluorometric measurements on these cells using a fluorescence microscope or in cell suspension using a fluorometer reveal that the roGFP1 probe is in dynamic equilibrium with the mitochondrial redox status and responds to membrane-permeable reductants and oxidants. The roGFP1 probe reports that the matrix space in HeLa cell mitochondria is highly reducing, with a midpoint potential near -360 mV (assuming mitochondrial pH approximately 8.0 at 37 degrees C). In other work (C. T. Dooley, T. M. Dore, G. Hanson, W. C. Jackson, S. J. Remington, and R. Y. Tsien, submitted for publication), it is shown that the cytosol of HeLa cells is also unusually reducing but somewhat less so than the mitochondrial matrix.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14722062}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14722062 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14722062}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Chromophore]]
[[Category: Chromophore]]
[[Category: Disulfide bond]]
[[Category: Disulfide bond]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:02:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:00:04 2008''

Revision as of 17:00, 1 July 2008

Image:1jc1.png

Template:STRUCTURE 1jc1

CRYSTAL STRUCTURE ANALYSIS OF A REDOX-SENSITIVE GREEN FLUORESCENT PROTEIN VARIANT IN A OXIDIZED FORM

Template:ABSTRACT PUBMED 14722062

About this Structure

1JC1 is a Single protein structure of sequence from Aequorea victoria. Full crystallographic information is available from OCA.

Reference

Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators., Hanson GT, Aggeler R, Oglesbee D, Cannon M, Capaldi RA, Tsien RY, Remington SJ, J Biol Chem. 2004 Mar 26;279(13):13044-53. Epub 2004 Jan 13. PMID:14722062

Page seeded by OCA on Tue Jul 1 20:00:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jc1"
Personal tools