1yyz
From Proteopedia
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|PDB= 1yyz |SIZE=350|CAPTION= <scene name='initialview01'>1yyz</scene>, resolution 1.85Å | |PDB= 1yyz |SIZE=350|CAPTION= <scene name='initialview01'>1yyz</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
| - | |ACTIVITY= [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] | + | |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= FBP1, FBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa]) | |GENE= FBP1, FBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1yxi|1YXI]], [[1yz0|1YZ0]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yyz OCA], [http://www.ebi.ac.uk/pdbsum/1yyz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yyz RCSB]</span> | ||
}} | }} | ||
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[[Category: Iancu, C V.]] | [[Category: Iancu, C V.]] | ||
[[Category: Mukund, S.]] | [[Category: Mukund, S.]] | ||
| - | [[Category: AMP]] | ||
| - | [[Category: F6P]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: 6-bisphosphatase]] | ||
[[Category: allostearic enzyme]] | [[Category: allostearic enzyme]] | ||
[[Category: fbpase]] | [[Category: fbpase]] | ||
| - | [[Category: fructose-1]] | + | [[Category: fructose-1,6-bisphosphatase]] |
[[Category: gluconeogenesis]] | [[Category: gluconeogenesis]] | ||
[[Category: glycolysis]] | [[Category: glycolysis]] | ||
[[Category: intermediate state]] | [[Category: intermediate state]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:26:38 2008'' |
Revision as of 22:26, 30 March 2008
| |||||||
| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | FBP1, FBP (Sus scrofa) | ||||||
| Activity: | Fructose-bisphosphatase, with EC number 3.1.3.11 | ||||||
| Related: | 1YXI, 1YZ0
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
R-State AMP Complex Reveals Initial Steps of the Quaternary Transition of Fructose-1,6-bisphosphatase
Overview
AMP transforms fructose-1,6-bisphosphatase from its active R-state to its inactive T-state; however, the mechanism of that transformation is poorly understood. The mutation of Ala(54) to leucine destabilizes the T-state of fructose-1,6-bisphosphatase. The mutant enzyme retains wild-type levels of activity, but the concentration of AMP that causes 50% inhibition increases 50-fold. In the absence of AMP, the Leu(54) enzyme adopts an R-state conformation nearly identical to that of the wild-type enzyme. The mutant enzyme, however, grows in two crystal forms in the presence of saturating AMP. In one form, the AMP-bound tetramer is in a T-like conformation, whereas in the other form, the AMP-bound tetramer is in a R-like conformation. The latter reveals conformational changes in two helices due to the binding of AMP. Helix H1 moves toward the center of the tetramer and displaces Ile(10) from a hydrophobic pocket. The displacement of Ile(10) exposes a hydrophobic surface critical to interactions that stabilize the T-state. Helix H2 moves away from the center of the tetramer, breaking hydrogen bonds with a buried loop (residues 187-195) in an adjacent subunit. The same hydrogen bonds reform but only after the quaternary transition to the T-state. Proposed here is a model that accounts for the quaternary transition and cooperativity in the inhibition of catalysis by AMP.
About this Structure
1YYZ is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase., Iancu CV, Mukund S, Fromm HJ, Honzatko RB, J Biol Chem. 2005 May 20;280(20):19737-45. Epub 2005 Mar 14. PMID:15767255
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