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| - | [[Image:3bif.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_3bif| PDB=3bif | SCENE= }} | | {{STRUCTURE_3bif| PDB=3bif | SCENE= }} |
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| - | '''6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE EMPTY 6-PF-2K ACTIVE SITE'''
| + | ===6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE EMPTY 6-PF-2K ACTIVE SITE=== |
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| - | ==Overview==
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| - | The bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase plays an essential role in the regulation of glucose metabolism by both producing and degrading Fru-2,6-P(2) via its distinct catalytic activities. The 6-PF-2-K and Fru-2,6-P(2)ase active sites are located in separate domains of the enzyme. The kinase domain is structurally related to the superfamily of mononucleotide binding proteins that includes adenylate kinase and the G-proteins. We have determined three new structures of the enzymatic monomer, each with a different ligand in the ATP binding site of the 6-PF-2-K domain (AMP-PNP, PO(4), and water). A comparison of these three new structures with the ATPgammaS-bound 6-PF-2-K domain reveals a rearrangement of a helix that is dependent on the ligand bound in the ATP binding site of the enzyme. This helix motion dramatically alters the position of a catalytic residue (Lys172). This catalytic cation is analogous to the Arg residue donated by the rasGAP protein, and the Arg residue at the core of the GTP or GDP sensing switch motion seen in the heterotrimeric G-proteins. In addition, a succinate molecule is observed in the Fru-6-P binding site. Kinetic analysis of succinate inhibition of the 6-PF-2-K reaction is consistent with the structural findings, and suggests a mechanism for feedback inhibition of glycolysis by citric acid cycle intermediates. Alterations in the 6-PF-2-K kinetics of several proteins mutated near both the switch and the succinate binding site suggest a mode of communication between the ATP- and F6P binding sites. Together with these kinetic data, these new structures provide insights into the mechanism of the 6-PF-2-K activity of this important bifunctional enzyme. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10493801}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10493801 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10493801}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Phosphatase]] | | [[Category: Phosphatase]] |
| | [[Category: Phosphotransferase]] | | [[Category: Phosphotransferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:48:23 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:23:49 2008'' |
Revision as of 15:23, 27 July 2008
Template:STRUCTURE 3bif
6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE EMPTY 6-PF-2K ACTIVE SITE
Template:ABSTRACT PUBMED 10493801
About this Structure
3BIF is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
A switch in the kinase domain of rat testis 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase., Yuen MH, Wang XL, Mizuguchi H, Uyeda K, Hasemann CA, Biochemistry. 1999 Sep 21;38(38):12333-42. PMID:10493801
Page seeded by OCA on Sun Jul 27 18:23:49 2008
