From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2dwp.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:2dwp.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2dwp| PDB=2dwp | SCENE= }} | | {{STRUCTURE_2dwp| PDB=2dwp | SCENE= }} |
| | | | |
| - | '''A pseudo substrate complex of 6-phosphofructo-2-kinase of PFKFB'''
| + | ===A pseudo substrate complex of 6-phosphofructo-2-kinase of PFKFB=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | To understand the molecular basis of a phosphoryl transfer reaction catalyzed by the 6-phosphofructo-2-kinase domain of the hypoxia-inducible bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), the crystal structures of PFKFB3AMPPCPfructose-6-phosphate and PFKFB3ADPphosphoenolpyruvate complexes were determined to 2.7 A and 2.25 A resolution, respectively. Kinetic studies on the wild-type and site-directed mutant proteins were carried out to confirm the structural observations. The experimentally varied liganding states in the active pocket cause no significant conformational changes. In the pseudo-substrate complex, a strong direct interaction between AMPPCP and fructose-6-phosphate (Fru-6-P) is found. By virtue of this direct substrate-substrate interaction, Fru-6-P is aligned with AMPPCP in an orientation and proximity most suitable for a direct transfer of the gamma-phosphate moiety to 2-OH of Fru-6-P. The three key atoms involved in the phosphoryl transfer, the beta,gamma-phosphate bridge oxygen atom, the gamma-phosphorus atom, and the 2-OH group are positioned in a single line, suggesting a direct phosphoryl transfer without formation of a phosphoenzyme intermediate. In addition, the distance between 2-OH and gamma-phosphorus allows the gamma-phosphate oxygen atoms to serve as a general base catalyst to induce an "associative" phosphoryl transfer mechanism. The site-directed mutant study and inhibition kinetics suggest that this reaction will be catalyzed most efficiently by the protein when the substrates bind to the active pocket in an ordered manner in which ATP binds first.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17499765}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17499765 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17499765}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | [[Category: Transferase]] | | [[Category: Transferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 7 08:42:19 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:16:52 2008'' |
Revision as of 16:17, 27 July 2008
Template:STRUCTURE 2dwp
A pseudo substrate complex of 6-phosphofructo-2-kinase of PFKFB
Template:ABSTRACT PUBMED 17499765
About this Structure
2DWP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A direct substrate-substrate interaction found in the kinase domain of the bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase., Kim SG, Cavalier M, El-Maghrabi MR, Lee YH, J Mol Biol. 2007 Jun 29;370(1):14-26. Epub 2007 Mar 21. PMID:17499765
Page seeded by OCA on Sun Jul 27 19:16:52 2008
