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.


1ej3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ej3.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ej3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ej3| PDB=1ej3 | SCENE= }}
{{STRUCTURE_1ej3| PDB=1ej3 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF AEQUORIN'''
+
===CRYSTAL STRUCTURE OF AEQUORIN===
-
==Overview==
+
<!--
-
Aequorin is a calcium-sensitive photoprotein originally obtained from the jellyfish Aequorea aequorea. Because it has a high sensitivity to calcium ions and is biologically harmless, aequorin is widely used as a probe to monitor intracellular levels of free calcium. The aequorin molecule contains four helix-loop-helix 'EF-hand' domains, of which three can bind calcium. The molecule also contains coelenterazine as its chromophoric ligand. When calcium is added, the protein complex decomposes into apoaequorin, coelenteramide and CO2, accompanied by the emission of light. Apoaequorin can be regenerated into active aequorin in the absence of calcium by incubation with coelenterazine, oxygen and a thiol agent. Cloning and expression of the complementary DNA for aequorin were first reported in 1985 (refs 2, 6), and growth of crystals of the recombinant protein has been described; however, techniques have only recently been developed to prepare recombinant aequorin of the highest purity, permitting a full crystallographic study. Here we report the structure of recombinant aequorin determined by X-ray crystallography. Aequorin is found to be a globular molecule containing a hydrophobic core cavity that accommodates the ligand coelenterazine-2-hydroperoxide. The structure shows protein components stabilizing the peroxide and suggests a mechanism by which calcium activation may occur.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10830969}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10830969 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10830969}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Four ef-hand calcium-binding protein]]
[[Category: Four ef-hand calcium-binding protein]]
[[Category: Protein-coelenterazine peroxide complex]]
[[Category: Protein-coelenterazine peroxide complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:09:47 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:49:23 2008''

Revision as of 21:49, 30 June 2008

Image:1ej3.png

Template:STRUCTURE 1ej3

CRYSTAL STRUCTURE OF AEQUORIN

Template:ABSTRACT PUBMED 10830969

About this Structure

1EJ3 is a Single protein structure of sequence from Aequorea aequorea. Full crystallographic information is available from OCA.

Reference

The crystal structure of the photoprotein aequorin at 2.3 A resolution., Head JF, Inouye S, Teranishi K, Shimomura O, Nature. 2000 May 18;405(6784):372-6. PMID:10830969

Page seeded by OCA on Tue Jul 1 00:49:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ej3"
Personal tools