1nv7: Difference between revisions

Revision as of 01:44, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nv7.png

Template:STRUCTURE 1nv7

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

Template:ABSTRACT PUBMED 12595529

About this StructureAbout this Structure

1NV7 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

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 01:44:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1nv7.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1nv7|  PDB=1nv7  |  SCENE=  }}
-'''Fructose-1,6-Bisphosphatase Complex With AMP, Magnesium, Fructose-6-Phosphate, Phosphate and Thallium (20 mM)'''
+===Fructose-1,6-Bisphosphatase Complex With AMP, 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==
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 [[Category: Bisphosphatase]]
 [[Category: Gluconeogenesis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:01:11 2008''
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