From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2ox3.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:2ox3.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2ox3| PDB=2ox3 | SCENE= }} | | {{STRUCTURE_2ox3| PDB=2ox3 | SCENE= }} |
| | | | |
| - | '''R-state, PEP and Fru-6-P-bound, Escherichia coli fructose-1,6-bisphosphatase'''
| + | ===R-state, PEP and Fru-6-P-bound, Escherichia coli fructose-1,6-bisphosphatase=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The enteric bacterium Escherichia coli requires fructose-1,6-bisphosphatase (FBPase) for growth on gluconeogenic carbon sources. Constitutive expression of FBPase and fructose-6-phosphate-1-kinase coupled with the absence of futile cycling implies an undetermined mechanism of coordinate regulation involving both enzymes. Tricarboxylic acids and phosphorylated three-carbon carboxylic acids, all intermediates of glycolysis and the tricarboxylic acid cycle, are shown here to activate E. coli FBPase. The two most potent activators, phosphoenolpyruvate and citrate, bind to the sulfate anion site, revealed previously in the first crystal structure of the E. coli enzyme. Tetramers ligated with either phosphoenolpyruvate or citrate, in contrast to the sulfate-bound structure, are in the canonical R-state of porcine FBPase but nevertheless retain sterically blocked AMP pockets. At physiologically relevant concentrations, phosphoenolpyruvate and citrate stabilize an active tetramer over a less active enzyme form of mass comparable with that of a dimer. The above implies the conservation of the R-state through evolution. FBPases of heterotrophic organisms of distantly related phylogenetic groups retain residues of the allosteric activator site and in those instances where data are available exhibit activation by phosphoenolpyruvate. Findings here unify disparate observations regarding bacterial FBPases, implicating a mechanism of feed-forward activation in bacterial central metabolism. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17314096}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17314096 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17314096}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 35: |
Line 39: |
| | [[Category: Protein-protein interaction]] | | [[Category: Protein-protein interaction]] |
| | [[Category: Proteobacteria]] | | [[Category: Proteobacteria]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:50:50 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:36:20 2008'' |
Revision as of 12:36, 29 July 2008
Template:STRUCTURE 2ox3
R-state, PEP and Fru-6-P-bound, Escherichia coli fructose-1,6-bisphosphatase
Template:ABSTRACT PUBMED 17314096
About this Structure
2OX3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state., Hines JK, Fromm HJ, Honzatko RB, J Biol Chem. 2007 Apr 20;282(16):11696-704. Epub 2007 Feb 21. PMID:17314096
Page seeded by OCA on Tue Jul 29 15:36:20 2008
