1fpf: Difference between revisions

Revision as of 03:44, 1 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:1fpf.png

Template:STRUCTURE 1fpf

STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHYSTRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY

Template:ABSTRACT PUBMED 7703244

About this StructureAbout this Structure

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

ReferenceReference

Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography., Villeret V, Huang S, Zhang Y, Lipscomb WN, Biochemistry. 1995 Apr 4;34(13):4307-15. PMID:7703244

Page seeded by OCA on Tue Jul 1 03:44:04 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1fpf.jpg|left|200px]]
+{{Seed}}
+[[Image:1fpf.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1fpf|  PDB=1fpf  |  SCENE=  }}
-'''STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY'''
+===STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY===
-==Overview==
+<!--
-The crystal structures of the T form pig kidney fructose-1,6-bisphosphatase (EC 3.1.3.11) complexed with AMP, the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate (AhG-1,6-P2), and Mn2+ at concentrations of 5, 15, 100, and 300 microM have been determined and refined at resolutions of 2.1-2.3 A to R factors which range from 0.180 to 0.195, respectively. Two metal ions per active site have been identified, one at a binding site of high affinity (metal site 1'), the second in a low affinity site (metal site 2'). The 1-phosphate group of the substrate analogue coordinates to the metal ion at site 1', but not at site 2'. In these four complexes, the distances between the two metal ions are all within 0.2 A of 4.3 A. In the previously determined R form structure of Fru-1,6-Pase complexed with AhG-1,6-P2 and Mn2+, there are also two metal ions in the active site at metal sites 1 and 2. The metal ion at site 1 is only 0.6 A displaced from the metal ion at site 1' in the T form and is also coordinated to the 1-phosphate group of AhG-1,6-P2. However, the second metal ion is located in two distinct sites which are 1.4 A apart in the T and R form structures. In the R form the Mn2+ at site 2 is coordinated to the 1-phosphate group of the substrate analogue. This metal ion is apparently required to orient the phosphate group for nucleophilic attack at the phosphorus center.(ABSTRACT TRUNCATED AT 250 WORDS)
+The line below this paragraph, {{ABSTRACT_PUBMED_7703244}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7703244 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7703244}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Villeret, V.]]
 [[Category: Zhang, Y.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:36:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:44:04 2008''