PDBsum entry 1fpf

Hydrolase (phosphoric monoester)

PDB id: 1fpf

Contents

Protein chains

317 a.a. *

Ligands

AHG ×2

AMP ×2

Metals

_MN ×4

Waters ×468

* Residue conservation analysis

PDB id:

1fpf

Name:

Hydrolase (phosphoric monoester)

Title:

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

Structure:

Fructose 1,6-bisphosphatase. Chain: a, b. Engineered: yes

Source:

Sus scrofa. Pig. Organism_taxid: 9823

Biol. unit:

Tetramer (from PQS)

Resolution:

2.10Å R-factor: 0.183

Authors:

V.Villeret,S.Huang,Y.Zhang,W.N.Lipscomb

Key ref:

V.Villeret et al. (1995). 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. Biochemistry, 34, 4307-4315. PubMed id: 7703244 DOI: 10.1021/bi00013a020

Date:

15-Dec-94 Release date: 27-Feb-95

Protein chains

P00636  (F16P1_PIG) -  Fructose-1,6-bisphosphatase 1 from Sus scrofa

Seq: 338 a.a.

Struc: 317 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.1.3.11 - fructose-bisphosphatase.
• Pathway: Pentose Phosphate Pathway (later stages)
• Reaction: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate

beta-D-fructose 1,6-bisphosphate (Bound ligand (Het Group name = AHG) matches with 95.00% similarity) + H2O = beta-D-fructose 6-phosphate + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1021/bi00013a020

Biochemistry 34:4307-4315 (1995)

PubMed id: 7703244

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.

V.Villeret, S.Huang, Y.Zhang, W.N.Lipscomb.

ABSTRACT

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)