1nv2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nv2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1nv2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nv2| PDB=1nv2 | SCENE= }}
{{STRUCTURE_1nv2| PDB=1nv2 | SCENE= }}
-
'''Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6-Phosphate, Phosphate and Thallium (20 mM)'''
+
===Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6-Phosphate, Phosphate and Thallium (20 mM)===
-
==Overview==
+
<!--
-
Fructose-1,6-bisphosphatase requires divalent cations (Mg2+, Mn2+, or Zn2+) for catalysis, but a diverse set of monovalent cations (K+, Tl+, Rb+, or NH(4)(+)) will further enhance enzyme activity. Here, the interaction of Tl+ with fructose-1,6-bisphosphatase is explored under conditions that support catalysis. On the basis of initial velocity kinetics, Tl+ enhances catalysis by 20% with a K(a) of 1.3 mm and a Hill coefficient near unity. Crystal structures of enzyme complexes with Mg2+, Tl+, and reaction products, in which the concentration of Tl+ is 1 mm or less, reveal Mg2+ at metal sites 1, 2, and 3 of the active site, but little or no bound Tl+. Intermediate concentrations of Tl+ (5-20 mm) displace Mg2+ from site 3 and the 1-OH group of fructose 6-phosphate from in-line geometry with respect to bound orthophosphate. Loop 52-72 appears in a new conformational state, differing from its engaged conformation by disorder in residues 61-69. Tl+ does not bind to metal sites 1 or 2 in the presence of Mg2+, but does bind to four other sites with partial occupancy. Two of four Tl+ sites probably represent alternative binding sites for the site 3 catalytic Mg2+, whereas the other sites could play roles in monovalent cation activation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12595529}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12595529 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12595529}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Gluconeogenesis]]
[[Category: Gluconeogenesis]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:00:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:52:46 2008''

Revision as of 08:52, 29 July 2008

Image:1nv2.png

Template:STRUCTURE 1nv2

Fructose-1,6-Bisphosphatase Complex with Magnesium, Fructose-6-Phosphate, Phosphate and Thallium (20 mM)

Template:ABSTRACT PUBMED 12595529

About this Structure

1NV2 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Interaction of Tl+ with product complexes of fructose-1,6-bisphosphatase., Choe JY, Nelson SW, Fromm HJ, Honzatko RB, J Biol Chem. 2003 May 2;278(18):16008-14. Epub 2003 Feb 20. PMID:12595529

Page seeded by OCA on Tue Jul 29 11:52:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nv2"
Personal tools