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.


1eyk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1eyk.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1eyk.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1eyk| PDB=1eyk | SCENE= }}
{{STRUCTURE_1eyk| PDB=1eyk | SCENE= }}
-
'''FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, ZINC, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (T-STATE)'''
+
===FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, ZINC, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (T-STATE)===
-
==Overview==
+
<!--
-
Crystal structures of metal-product complexes of fructose 1, 6-bisphosphatase (FBPase) reveal competition between AMP and divalent cations. In the presence of AMP, the Zn(2+)-product and Mg(2+)-product complexes have a divalent cation present only at one of three metal binding sites (site 1). The enzyme is in the T-state conformation with a disordered loop of residues 52-72 (loop 52-72). In the absence of AMP, the enzyme crystallizes in the R-state conformation, with loop 52-72 associated with the active site. In structures without AMP, three metal-binding sites are occupied by Zn(2+) and two of three metal sites (sites 1 and 2) by Mg(2+). Evidently, the association of AMP with FBPase disorders loop 52-72, the consequence of which is the release of cations from two of three metal binding sites. In the Mg(2+) complexes (but not the Zn(2+) complexes), the 1-OH group of fructose 6-phosphate (F6P) coordinates to the metal at site 1 and is oriented for a nucleophilic attack on the bound phosphate molecule. A mechanism is presented for the forward reaction, in which Asp74 and Glu98 together generate a hydroxide anion coordinated to the Mg(2+) at site 2, which then displaces F6P. Development of negative charge on the 1-oxygen of F6P is stabilized by its coordination to the Mg(2+) at site 1.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10913263}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10913263 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10913263}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Bisphosphatase]]
[[Category: Bisphosphatase]]
[[Category: Gluconeogenesis]]
[[Category: Gluconeogenesis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:40:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:13:01 2008''

Revision as of 23:13, 30 June 2008

Image:1eyk.png

Template:STRUCTURE 1eyk

FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, ZINC, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (T-STATE)

Template:ABSTRACT PUBMED 10913263

About this Structure

1EYK is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes., Choe JY, Fromm HJ, Honzatko RB, Biochemistry. 2000 Jul 25;39(29):8565-74. PMID:10913263

Page seeded by OCA on Tue Jul 1 02:13:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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