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1eyj

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(New page: 200px<br /><applet load="1eyj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eyj, resolution 2.28&Aring;" /> '''FRUCTOSE-1,6-BISPHOS...)
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'''FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, MAGNESIUM, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (T-STATE)'''<br />
'''FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, MAGNESIUM, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (T-STATE)'''<br />
==Overview==
==Overview==
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Crystal structures of metal-product complexes of fructose 1, 6-bisphosphatase (FBPase) reveal competition between AMP and divalent, cations. In the presence of AMP, the Zn(2+)-product and Mg(2+)-product, complexes have a divalent cation present only at one of three metal, binding sites (site 1). The enzyme is in the T-state conformation with a, disordered loop of residues 52-72 (loop 52-72). In the absence of AMP, the, enzyme crystallizes in the R-state conformation, with loop 52-72, associated with the active site. In structures without AMP, three, metal-binding sites are occupied by Zn(2+) and two of three metal sites, (sites 1 and 2) by Mg(2+). Evidently, the association of AMP with FBPase, disorders loop 52-72, the consequence of which is the release of cations, from two of three metal binding sites. In the Mg(2+) complexes (but not, the Zn(2+) complexes), the 1-OH group of fructose 6-phosphate (F6P), coordinates to the metal at site 1 and is oriented for a nucleophilic, attack on the bound phosphate molecule. A mechanism is presented for the, forward reaction, in which Asp74 and Glu98 together generate a hydroxide, anion coordinated to the Mg(2+) at site 2, which then displaces F6P., Development of negative charge on the 1-oxygen of F6P is stabilized by its, coordination to the Mg(2+) at site 1.
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Crystal structures of metal-product complexes of fructose 1, 6-bisphosphatase (FBPase) reveal competition between AMP and divalent cations. In the presence of AMP, the Zn(2+)-product and Mg(2+)-product complexes have a divalent cation present only at one of three metal binding sites (site 1). The enzyme is in the T-state conformation with a disordered loop of residues 52-72 (loop 52-72). In the absence of AMP, the enzyme crystallizes in the R-state conformation, with loop 52-72 associated with the active site. In structures without AMP, three metal-binding sites are occupied by Zn(2+) and two of three metal sites (sites 1 and 2) by Mg(2+). Evidently, the association of AMP with FBPase disorders loop 52-72, the consequence of which is the release of cations from two of three metal binding sites. In the Mg(2+) complexes (but not the Zn(2+) complexes), the 1-OH group of fructose 6-phosphate (F6P) coordinates to the metal at site 1 and is oriented for a nucleophilic attack on the bound phosphate molecule. A mechanism is presented for the forward reaction, in which Asp74 and Glu98 together generate a hydroxide anion coordinated to the Mg(2+) at site 2, which then displaces F6P. Development of negative charge on the 1-oxygen of F6P is stabilized by its coordination to the Mg(2+) at site 1.
==About this Structure==
==About this Structure==
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1EYJ 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, MG, PO4 and AMP as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EYJ OCA].
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1EYJ 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>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1EYJ OCA].
==Reference==
==Reference==
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Choe, J.]]
[[Category: Choe, J.]]
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[[Category: Honzatko, R.B.]]
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[[Category: Honzatko, R B.]]
[[Category: AMP]]
[[Category: AMP]]
[[Category: F6P]]
[[Category: F6P]]
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[[Category: gluconeogenesis]]
[[Category: gluconeogenesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:26:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:52 2008''

Revision as of 10:32, 21 February 2008

Image:1eyj.jpg

1eyj, resolution 2.28Å

Drag the structure with the mouse to rotate

FRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, MAGNESIUM, FRUCTOSE-6-PHOSPHATE AND PHOSPHATE (T-STATE)

Overview

Crystal structures of metal-product complexes of fructose 1, 6-bisphosphatase (FBPase) reveal competition between AMP and divalent cations. In the presence of AMP, the Zn(2+)-product and Mg(2+)-product complexes have a divalent cation present only at one of three metal binding sites (site 1). The enzyme is in the T-state conformation with a disordered loop of residues 52-72 (loop 52-72). In the absence of AMP, the enzyme crystallizes in the R-state conformation, with loop 52-72 associated with the active site. In structures without AMP, three metal-binding sites are occupied by Zn(2+) and two of three metal sites (sites 1 and 2) by Mg(2+). Evidently, the association of AMP with FBPase disorders loop 52-72, the consequence of which is the release of cations from two of three metal binding sites. In the Mg(2+) complexes (but not the Zn(2+) complexes), the 1-OH group of fructose 6-phosphate (F6P) coordinates to the metal at site 1 and is oriented for a nucleophilic attack on the bound phosphate molecule. A mechanism is presented for the forward reaction, in which Asp74 and Glu98 together generate a hydroxide anion coordinated to the Mg(2+) at site 2, which then displaces F6P. Development of negative charge on the 1-oxygen of F6P is stabilized by its coordination to the Mg(2+) at site 1.

About this Structure

1EYJ is a Single protein structure of sequence from Sus scrofa with , , and as ligands. Active as Fructose-bisphosphatase, with EC number 3.1.3.11 Full crystallographic information is available from OCA.

Reference

Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes., Choe JY, Fromm HJ, Honzatko RB, Biochemistry. 2000 Jul 25;39(29):8565-74. PMID:10913263

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