1g98: Difference between revisions

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[[Image:1g98.jpg|left|200px]]<br /><applet load="1g98" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1g98.jpg|left|200px]]<br /><applet load="1g98" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1g98, resolution 1.9Å" />

'''CRYSTAL STRUCTURE ANALYSIS OF RABBIT PHOSPHOGLUCOSE ISOMERASE COMPLEXED WITH 5-PHOSPHOARABINONATE, A TRANSITION STATE ANALOGUE'''<br />

==Overview==

Phosphoglucose isomerase (PGI; E.C. 5.3.1.9) catalyzes the second step in, glycolysis, the interconversion of D-glucose-6-phosphate and, D-fructose-6-phosphate. We determined the X-ray crystal structure of, rabbit PGI complexed with a competitive inhibitor of isomerase activity, 5-phospho-D-arabinonate (5PAA), at 1.9 A resolution. 5PAA is a better, mimic of the proposed cis-enediol(ate) intermediate than, 6-phospho-D-gluconate, which was used in a previously reported crystal, structure of rabbit PGI. The orientation of 5PAA bound in the enzyme, active site predicts that active site residue Glu357 is the residue that, transfers a proton between C2 and C1 of the proposed cis-enediol(ate), intermediate. Amino acid residues Arg272 and Lys210 are predicted to be, involved in stabilizing the negative charge of the intermediate.

Phosphoglucose isomerase (PGI; E.C. 5.3.1.9) catalyzes the second step in glycolysis, the interconversion of D-glucose-6-phosphate and D-fructose-6-phosphate. We determined the X-ray crystal structure of rabbit PGI complexed with a competitive inhibitor of isomerase activity, 5-phospho-D-arabinonate (5PAA), at 1.9 A resolution. 5PAA is a better mimic of the proposed cis-enediol(ate) intermediate than 6-phospho-D-gluconate, which was used in a previously reported crystal structure of rabbit PGI. The orientation of 5PAA bound in the enzyme active site predicts that active site residue Glu357 is the residue that transfers a proton between C2 and C1 of the proposed cis-enediol(ate) intermediate. Amino acid residues Arg272 and Lys210 are predicted to be involved in stabilizing the negative charge of the intermediate.

==About this Structure==

1G98 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with PA5 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1G98 OCA].

1G98 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=PA5:'>PA5</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G98 OCA].

==Reference==

Line 15:

[[Category: Single protein]]

[[Category: Hardre, R.]]

[[Category: Jeffery, C.J.]]

[[Category: Jeffery, C J.]]

[[Category: Salmon, L.]]

[[Category: PA5]]

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[[Category: transition state analogue]]

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@@ Line 1: / Line 1: @@
-[[Image:1g98.jpg|left|200px]]<br /><applet load="1g98" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1g98.jpg|left|200px]]<br /><applet load="1g98" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1g98, resolution 1.9&Aring;" />
 '''CRYSTAL STRUCTURE ANALYSIS OF RABBIT PHOSPHOGLUCOSE ISOMERASE COMPLEXED WITH 5-PHOSPHOARABINONATE, A TRANSITION STATE ANALOGUE'''<br />
 ==Overview==
-Phosphoglucose isomerase (PGI; E.C. 5.3.1.9) catalyzes the second step in, glycolysis, the interconversion of D-glucose-6-phosphate and, D-fructose-6-phosphate. We determined the X-ray crystal structure of, rabbit PGI complexed with a competitive inhibitor of isomerase activity, 5-phospho-D-arabinonate (5PAA), at 1.9 A resolution. 5PAA is a better, mimic of the proposed cis-enediol(ate) intermediate than, 6-phospho-D-gluconate, which was used in a previously reported crystal, structure of rabbit PGI. The orientation of 5PAA bound in the enzyme, active site predicts that active site residue Glu357 is the residue that, transfers a proton between C2 and C1 of the proposed cis-enediol(ate), intermediate. Amino acid residues Arg272 and Lys210 are predicted to be, involved in stabilizing the negative charge of the intermediate.
+Phosphoglucose isomerase (PGI; E.C. 5.3.1.9) catalyzes the second step in glycolysis, the interconversion of D-glucose-6-phosphate and D-fructose-6-phosphate. We determined the X-ray crystal structure of rabbit PGI complexed with a competitive inhibitor of isomerase activity, 5-phospho-D-arabinonate (5PAA), at 1.9 A resolution. 5PAA is a better mimic of the proposed cis-enediol(ate) intermediate than 6-phospho-D-gluconate, which was used in a previously reported crystal structure of rabbit PGI. The orientation of 5PAA bound in the enzyme active site predicts that active site residue Glu357 is the residue that transfers a proton between C2 and C1 of the proposed cis-enediol(ate) intermediate. Amino acid residues Arg272 and Lys210 are predicted to be involved in stabilizing the negative charge of the intermediate.
 ==About this Structure==
-G98 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with PA5 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G98 OCA].
+G98 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=PA5:'>PA5</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G98 OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Hardre, R.]]
-[[Category: Jeffery, C.J.]]
+[[Category: Jeffery, C J.]]
 [[Category: Salmon, L.]]
 [[Category: PA5]]
@@ Line 22: / Line 22: @@
 [[Category: transition state analogue]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:50:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:33 2008''