1frp: Difference between revisions
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|PDB= 1frp |SIZE=350|CAPTION= <scene name='initialview01'>1frp</scene>, resolution 2.0Å | |PDB= 1frp |SIZE=350|CAPTION= <scene name='initialview01'>1frp</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] </span> | |||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1frp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frp OCA], [http://www.ebi.ac.uk/pdbsum/1frp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1frp RCSB]</span> | |||
}} | }} | ||
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[[Category: Xue, Y.]] | [[Category: Xue, Y.]] | ||
[[Category: Zhang, Y.]] | [[Category: Zhang, Y.]] | ||
[[Category: hydrolase(phosphoric monoester)]] | [[Category: hydrolase(phosphoric monoester)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:28:58 2008'' | ||
Revision as of 20:28, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | , , | ||||||
| Activity: | Fructose-bisphosphatase, with EC number 3.1.3.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
OverviewOverview
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.
About this StructureAbout this Structure
1FRP is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
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., Xue Y, Huang S, Liang JY, Zhang Y, Lipscomb WN, Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12482-6. PMID:7809062
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