1rya: Difference between revisions

Line 1:

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

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

caption="1rya, resolution 1.30Å" />

'''Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG'''<br />

==Overview==

GDP-mannose glycosyl hydrolase (GDPMH) catalyzes the hydrolysis of, GDP-mannose and GDP-glucose to GDP and sugar by substitution with, inversion at C1 of the sugar. The enzyme has a modified Nudix motif and, requires one divalent cation for activity. The 1.3 A X-ray structure of, the GDPMH-Mg(2+)-GDP complex, together with kinetic, mutational, and NMR, data, suggests a mechanism for the GDPMH reaction. Several residues and, the divalent cation strongly promote the departure of the GDP leaving, group, supporting a dissociative mechanism. Comparison of the GDPMH, structure with that of a typical Nudix hydrolase suggests how sequence, changes result in the switch of catalytic activity from P-O bond cleavage, to C-O bond cleavage. Changes in the Nudix motif result in loss of binding, of at least one Mg(2+) ion, and shortening of a loop by 6 residues shifts, the catalytic base by approximately 10 A.

GDP-mannose glycosyl hydrolase (GDPMH) catalyzes the hydrolysis of GDP-mannose and GDP-glucose to GDP and sugar by substitution with inversion at C1 of the sugar. The enzyme has a modified Nudix motif and requires one divalent cation for activity. The 1.3 A X-ray structure of the GDPMH-Mg(2+)-GDP complex, together with kinetic, mutational, and NMR data, suggests a mechanism for the GDPMH reaction. Several residues and the divalent cation strongly promote the departure of the GDP leaving group, supporting a dissociative mechanism. Comparison of the GDPMH structure with that of a typical Nudix hydrolase suggests how sequence changes result in the switch of catalytic activity from P-O bond cleavage to C-O bond cleavage. Changes in the Nudix motif result in loss of binding of at least one Mg(2+) ion, and shortening of a loop by 6 residues shifts the catalytic base by approximately 10 A.

==About this Structure==

1RYA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, CL, GDP and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1RYA OCA].

1RYA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=GDP:'>GDP</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RYA OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Amzel, L.M.]]

[[Category: Amzel, L M.]]

[[Category: Bianchet, M.A.]]

[[Category: Bianchet, M A.]]

[[Category: Gabelli, S.B.]]

[[Category: Gabelli, S B.]]

[[Category: Legler, P.M.]]

[[Category: Legler, P M.]]

[[Category: Mildvan, A.S.]]

[[Category: Mildvan, A S.]]

[[Category: CL]]

[[Category: GDP]]

Line 28:

[[Category: nudix mg-complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 01:57:~~16 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:51 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1rya.jpg|left|200px]]<br /><applet load="1rya" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rya.jpg|left|200px]]<br /><applet load="1rya" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rya, resolution 1.30&Aring;" />
 '''Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG'''<br />
 ==Overview==
-GDP-mannose glycosyl hydrolase (GDPMH) catalyzes the hydrolysis of, GDP-mannose and GDP-glucose to GDP and sugar by substitution with, inversion at C1 of the sugar. The enzyme has a modified Nudix motif and, requires one divalent cation for activity. The 1.3 A X-ray structure of, the GDPMH-Mg(2+)-GDP complex, together with kinetic, mutational, and NMR, data, suggests a mechanism for the GDPMH reaction. Several residues and, the divalent cation strongly promote the departure of the GDP leaving, group, supporting a dissociative mechanism. Comparison of the GDPMH, structure with that of a typical Nudix hydrolase suggests how sequence, changes result in the switch of catalytic activity from P-O bond cleavage, to C-O bond cleavage. Changes in the Nudix motif result in loss of binding, of at least one Mg(2+) ion, and shortening of a loop by 6 residues shifts, the catalytic base by approximately 10 A.
+GDP-mannose glycosyl hydrolase (GDPMH) catalyzes the hydrolysis of GDP-mannose and GDP-glucose to GDP and sugar by substitution with inversion at C1 of the sugar. The enzyme has a modified Nudix motif and requires one divalent cation for activity. The 1.3 A X-ray structure of the GDPMH-Mg(2+)-GDP complex, together with kinetic, mutational, and NMR data, suggests a mechanism for the GDPMH reaction. Several residues and the divalent cation strongly promote the departure of the GDP leaving group, supporting a dissociative mechanism. Comparison of the GDPMH structure with that of a typical Nudix hydrolase suggests how sequence changes result in the switch of catalytic activity from P-O bond cleavage to C-O bond cleavage. Changes in the Nudix motif result in loss of binding of at least one Mg(2+) ion, and shortening of a loop by 6 residues shifts the catalytic base by approximately 10 A.
 ==About this Structure==
-RYA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, CL, GDP and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RYA OCA].
+RYA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=GDP:'>GDP</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RYA OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Amzel, L.M.]]
+[[Category: Amzel, L M.]]
-[[Category: Bianchet, M.A.]]
+[[Category: Bianchet, M A.]]
-[[Category: Gabelli, S.B.]]
+[[Category: Gabelli, S B.]]
-[[Category: Legler, P.M.]]
+[[Category: Legler, P M.]]
-[[Category: Mildvan, A.S.]]
+[[Category: Mildvan, A S.]]
 [[Category: CL]]
 [[Category: GDP]]
@@ Line 28: / Line 28: @@
 [[Category: nudix mg-complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:57:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:51 2008''