1fbg: Difference between revisions

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CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE

OverviewOverview

The crystal structures of fructose-1,6-bisphosphatase (EC 3.1.3.11) complexed with substrate alone or with substrate analogues in the presence of divalent metal ions have been determined. The substrate analogues, 2,5-anhydro-D-glucitol-1,6-bisphosphate (AhG-1,6-P2) and 2,5-anhydro-D-mannitol-1,6-bisphosphate (AhM-1,6-P2), differ from the alpha and beta anomers of fructose-1,6-bisphosphate (Fru-1,6-P2), respectively, in that the OH on C2 is replaced by a hydrogen atom. Structures have been refined at resolutions of 2.5 to 3.0 A to R factors of 0.172 to 0.195 with root-mean-square deviations of 0.012-0.018 A and 2.7-3.8 degrees from the ideal geometries of bond lengths and bond angles, respectively. In addition, the complex of substrate with the enzyme has been determined in the absence of metal. The electron density at 2.5-A resolution does not distinguish between alpha and beta anomers, which differ for the most part only in the position of the 1-phosphate group and the orientation of the C2-hydroxyl group. The positions of the 6-phosphate and the sugar ring of the substrate analogues are almost identical to those of the respective anomer of the substrate. In the presence of metal ions the positions of the 1-phosphate groups of both alpha and beta analogues differ significantly (0.8-1.0 A) from those of anomers of the substrate in the metal-free complex. Two metal ions (Mn2+ or Zn2+) are located at the enzyme active site of complexes of the alpha analogue AhG-1,6-P2. Metal site 1 is coordinated by the carboxylate groups of Glu-97, Asp-118, and Glu-280 and the 1-phosphate group of substrate analogue, while the metal site 2 is coordinated by the carboxylate groups of Glu-97, Asp-118, the 1-phosphate group of substrate analogue, and the carbonyl oxygen of Leu-120. Both metal sites have a distorted tetrahedral geometry. However, only one metal ion (Mg2+ or Mn2+) is found very near the metal site 1 in the enzyme's active site in complexes of the beta analogue AhM-1,6-P2 or for Mg2+ in the complex of the alpha analogue AhG-1,6-P2. This single metal ion is coordinated by the carboxylate groups of Glu-97, Asp-118, Asp-121, and Glu-280 and the 1-phosphate group of substrate analogue in a distorted square pyramidal geometry.(ABSTRACT TRUNCATED AT 400 WORDS)

About this StructureAbout this Structure

1FBG 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.

ReferenceReference

Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase., Zhang Y, Liang JY, Huang S, Ke H, Lipscomb WN, Biochemistry. 1993 Feb 23;32(7):1844-57. PMID:8382525

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-[[Image:1fbg.jpg|left|200px]]<br /><applet load="1fbg" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fbg.jpg|left|200px]]<br /><applet load="1fbg" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fbg, resolution 3.0&Aring;" />
 '''CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE'''<br />
 ==Overview==
-The crystal structures of fructose-1,6-bisphosphatase (EC 3.1.3.11), complexed with substrate alone or with substrate analogues in the presence, of divalent metal ions have been determined. The substrate analogues, 2,5-anhydro-D-glucitol-1,6-bisphosphate (AhG-1,6-P2) and, 2,5-anhydro-D-mannitol-1,6-bisphosphate (AhM-1,6-P2), differ from the, alpha and beta anomers of fructose-1,6-bisphosphate (Fru-1,6-P2), respectively, in that the OH on C2 is replaced by a hydrogen atom., Structures have been refined at resolutions of 2.5 to 3.0 A to R factors, of 0.172 to 0.195 with root-mean-square deviations of 0.012-0.018 A and, 2.7-3.8 degrees from the ideal geometries of bond lengths and bond angles, respectively. In addition, the complex of substrate with the enzyme has, been determined in the absence of metal. The electron density at 2.5-A, resolution does not distinguish between alpha and beta anomers, which, differ for the most part only in the position of the 1-phosphate group and, the orientation of the C2-hydroxyl group. The positions of the 6-phosphate, and the sugar ring of the substrate analogues are almost identical to, those of the respective anomer of the substrate. In the presence of metal, ions the positions of the 1-phosphate groups of both alpha and beta, analogues differ significantly (0.8-1.0 A) from those of anomers of the, substrate in the metal-free complex. Two metal ions (Mn2+ or Zn2+) are, located at the enzyme active site of complexes of the alpha analogue, AhG-1,6-P2. Metal site 1 is coordinated by the carboxylate groups of, Glu-97, Asp-118, and Glu-280 and the 1-phosphate group of substrate, analogue, while the metal site 2 is coordinated by the carboxylate groups, of Glu-97, Asp-118, the 1-phosphate group of substrate analogue, and the, carbonyl oxygen of Leu-120. Both metal sites have a distorted tetrahedral, geometry. However, only one metal ion (Mg2+ or Mn2+) is found very near, the metal site 1 in the enzyme's active site in complexes of the beta, analogue AhM-1,6-P2 or for Mg2+ in the complex of the alpha analogue, AhG-1,6-P2. This single metal ion is coordinated by the carboxylate groups, of Glu-97, Asp-118, Asp-121, and Glu-280 and the 1-phosphate group of, substrate analogue in a distorted square pyramidal geometry.(ABSTRACT, TRUNCATED AT 400 WORDS)
+The crystal structures of fructose-1,6-bisphosphatase (EC 3.1.3.11) complexed with substrate alone or with substrate analogues in the presence of divalent metal ions have been determined. The substrate analogues, 2,5-anhydro-D-glucitol-1,6-bisphosphate (AhG-1,6-P2) and 2,5-anhydro-D-mannitol-1,6-bisphosphate (AhM-1,6-P2), differ from the alpha and beta anomers of fructose-1,6-bisphosphate (Fru-1,6-P2), respectively, in that the OH on C2 is replaced by a hydrogen atom. Structures have been refined at resolutions of 2.5 to 3.0 A to R factors of 0.172 to 0.195 with root-mean-square deviations of 0.012-0.018 A and 2.7-3.8 degrees from the ideal geometries of bond lengths and bond angles, respectively. In addition, the complex of substrate with the enzyme has been determined in the absence of metal. The electron density at 2.5-A resolution does not distinguish between alpha and beta anomers, which differ for the most part only in the position of the 1-phosphate group and the orientation of the C2-hydroxyl group. The positions of the 6-phosphate and the sugar ring of the substrate analogues are almost identical to those of the respective anomer of the substrate. In the presence of metal ions the positions of the 1-phosphate groups of both alpha and beta analogues differ significantly (0.8-1.0 A) from those of anomers of the substrate in the metal-free complex. Two metal ions (Mn2+ or Zn2+) are located at the enzyme active site of complexes of the alpha analogue AhG-1,6-P2. Metal site 1 is coordinated by the carboxylate groups of Glu-97, Asp-118, and Glu-280 and the 1-phosphate group of substrate analogue, while the metal site 2 is coordinated by the carboxylate groups of Glu-97, Asp-118, the 1-phosphate group of substrate analogue, and the carbonyl oxygen of Leu-120. Both metal sites have a distorted tetrahedral geometry. However, only one metal ion (Mg2+ or Mn2+) is found very near the metal site 1 in the enzyme's active site in complexes of the beta analogue AhM-1,6-P2 or for Mg2+ in the complex of the alpha analogue AhG-1,6-P2. This single metal ion is coordinated by the carboxylate groups of Glu-97, Asp-118, Asp-121, and Glu-280 and the 1-phosphate group of substrate analogue in a distorted square pyramidal geometry.(ABSTRACT TRUNCATED AT 400 WORDS)
 ==About this Structure==
-FBG 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 MN and AHM 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=1FBG OCA].
+FBG 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=MN:'>MN</scene> and <scene name='pdbligand=AHM:'>AHM</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=1FBG OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Huang, S.]]
 [[Category: Ke, H.]]
-[[Category: Liang, J.Y.]]
+[[Category: Liang, J Y.]]
-[[Category: Lipscomb, W.N.]]
+[[Category: Lipscomb, W N.]]
 [[Category: Zhang, Y.]]
 [[Category: AHM]]
@@ Line 23: / Line 23: @@
 [[Category: hydrolase(phosphoric monoester)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:47:24 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:56 2008''