PDBsum entry 1frp

Hydrolase(phosphoric monoester)

PDB id: 1frp

Contents

Protein chains

321 a.a. *

Ligands

FDP ×2

AMP ×2

Metals

_ZN ×2

Waters ×717

* Residue conservation analysis

PDB id:

1frp

Name:

Hydrolase(phosphoric monoester)

Title:

Crystal structure of fructose-1,6-bisphosphatase complexed with fructose-2,6-bisphosphate, amp and zn2+ at 2.0 angstroms resolution. Aspects of synergism between inhibitors

Structure:

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

Source:

Sus scrofa. Pig. Organism_taxid: 9823

Biol. unit:

Tetramer (from PQS)

Resolution:

2.00Å R-factor: 0.189

Authors:

Y.Xue,S.Huang,J.-Y.Liang,Y.Zhang,W.N.Lipscomb

Key ref:

Y.Xue et al. (1994). Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 2,6-bisphosphate, AMP, and Zn2+ at 2.0-A resolution: aspects of synergism between inhibitors. Proc Natl Acad Sci U S A, 91, 12482-12486. PubMed id: 7809062 DOI: 10.1073/pnas.91.26.12482

Date:

26-Aug-94 Release date: 30-Nov-94

Protein chains

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

Seq: 338 a.a.

Struc: 321 a.a.*

* PDB and UniProt seqs differ at 4 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 + H2O = beta-D-fructose 6-phosphate (Bound ligand (Het Group name = FDP) matches with 80.00% similarity) + phosphate

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

reference

DOI no: 10.1073/pnas.91.26.12482

Proc Natl Acad Sci U S A 91:12482-12486 (1994)

PubMed id: 7809062

Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 2,6-bisphosphate, AMP, and Zn2+ at 2.0-A resolution: aspects of synergism between inhibitors.

Y.Xue, S.Huang, J.Y.Liang, Y.Zhang, W.N.Lipscomb.

ABSTRACT

The crystal structure of fructose-1,6-bisphosphatase (Fru-1,6-Pase; EC 3.1.3.11) complexed with Zn2+ and two allosteric regulators, AMP and fructose 2,6-bisphosphate (Fru-2,6-P2) has been determined at 2.0-A resolution. In the refined model, the crystallographic R factor is 0.189 with rms deviations of 0.014 A and 2.8 degrees from ideal geometries for bond lengths and bond angles, respectively. A 15 degrees rotation is observed between the upper dimer C1C2 and the lower dimer C3C4 relative to the R-form structure (fructose 6-phosphate complex), consistent with that expected from a T-form structure. The major difference between the structure of the previously determined Fru-2,6-P2 complex (R form) and that of the current quaternary T-form complex lies in the active site domain. A zinc binding site distinct from the three binding sites established earlier was identified within each monomer. Helix H4 (residues 123-127) was found to be better defined than in previously studied ligated Fru-1,6-Pase structures. Interactions between monomers in the active site domain were found involving H4 residues from one monomer and residues Tyr-258 and Arg-243 from the adjacent monomer. Cooperativity between AMP and Fru-2,6-P2 in signal transmission probably involves the following features: an AMP site, the adjacent B3 strand (residues 113-118), the metal site, the immediate active site, the short helix H4 (residues 123-127), and Tyr-258 and Arg-243 from the adjacent monomer within the upper (or lower) dimer. The closest distance between the immediate active site and that on the adjacent monomer is only 5 A. Thus, the involvement of H4 in signal transmission adds another important pathway to the scheme of the allosteric mechanism of Fru-1,6-Pase.