5fbp
From Proteopedia
(New page: 200px<br /><applet load="5fbp" size="450" color="white" frame="true" align="right" spinBox="true" caption="5fbp, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:5fbp.gif|left|200px]]<br /><applet load="5fbp" size=" | + | [[Image:5fbp.gif|left|200px]]<br /><applet load="5fbp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="5fbp, resolution 2.1Å" /> | caption="5fbp, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH THE PRODUCT FRUCTOSE 6-PHOSPHATE AT 2.1-ANGSTROMS RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH THE PRODUCT FRUCTOSE 6-PHOSPHATE AT 2.1-ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of fructose-1,6-bisphosphatase (EC 3.1.3.11) | + | The crystal structure of fructose-1,6-bisphosphatase (EC 3.1.3.11) complexed with the product fructose 6-phosphate (F6P) has been refined at 2.1-A resolution to an R factor of 0.177 with root-mean-square deviations of 0.014 A and 2.9 degrees from the ideal geometries of bond lengths and bond angles, respectively. The secondary structures but not the trace of the unligated enzyme have been slightly revised in the F6P complex at this higher resolution. Helix H4 in the unligated structure has been refined to a helix-like coil, and two very short 3(10) helices have been found, one in H4 and one in H5. F6P at 10 mM concentration in the absence of divalent metals in our study shows major binding at the active site and minor binding at the AMP site. The major site has almost equal full occupancy in the C1 and C2 chains of the crystallographic asymmetric unit, while the minor site shows occupancy only in the C1 chain at about 50%. The electron density in both (2Fo - Fc) and (Fo - Fc) maps calculated by omitting F6P slightly favors the beta anomer of D-F6P over the alpha anomer. Possible functions of the active-site residues are discussed, and candidates are suggested for site-directed mutagenesis. |
==About this Structure== | ==About this Structure== | ||
| - | 5FBP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with F6P as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 5FBP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=F6P:'>F6P</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FBP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Ke, H.]] | [[Category: Ke, H.]] | ||
| - | [[Category: Liang, J | + | [[Category: Liang, J Y.]] |
| - | [[Category: Lipscomb, W | + | [[Category: Lipscomb, W N.]] |
[[Category: Zhang, Y.]] | [[Category: Zhang, Y.]] | ||
[[Category: F6P]] | [[Category: F6P]] | ||
[[Category: hydrolase (phosphoric monoester)]] | [[Category: hydrolase (phosphoric monoester)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:10 2008'' |
Revision as of 17:15, 21 February 2008
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CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH THE PRODUCT FRUCTOSE 6-PHOSPHATE AT 2.1-ANGSTROMS RESOLUTION
Overview
The crystal structure of fructose-1,6-bisphosphatase (EC 3.1.3.11) complexed with the product fructose 6-phosphate (F6P) has been refined at 2.1-A resolution to an R factor of 0.177 with root-mean-square deviations of 0.014 A and 2.9 degrees from the ideal geometries of bond lengths and bond angles, respectively. The secondary structures but not the trace of the unligated enzyme have been slightly revised in the F6P complex at this higher resolution. Helix H4 in the unligated structure has been refined to a helix-like coil, and two very short 3(10) helices have been found, one in H4 and one in H5. F6P at 10 mM concentration in the absence of divalent metals in our study shows major binding at the active site and minor binding at the AMP site. The major site has almost equal full occupancy in the C1 and C2 chains of the crystallographic asymmetric unit, while the minor site shows occupancy only in the C1 chain at about 50%. The electron density in both (2Fo - Fc) and (Fo - Fc) maps calculated by omitting F6P slightly favors the beta anomer of D-F6P over the alpha anomer. Possible functions of the active-site residues are discussed, and candidates are suggested for site-directed mutagenesis.
About this Structure
5FBP is a Single protein structure of sequence from Sus scrofa with as ligand. Active as Fructose-bisphosphatase, with EC number 3.1.3.11 Full crystallographic information is available from OCA.
Reference
Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-A resolution., Ke HM, Zhang YP, Liang JY, Lipscomb WN, Proc Natl Acad Sci U S A. 1991 Apr 15;88(8):2989-93. PMID:1849642
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