1rya
From Proteopedia
(New page: 200px<br /><applet load="1rya" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rya, resolution 1.30Å" /> '''Crystal Structure of...) |
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| - | [[Image:1rya.jpg|left|200px]]<br /><applet load="1rya" size=" | + | [[Image:1rya.jpg|left|200px]]<br /><applet load="1rya" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rya, resolution 1.30Å" /> | caption="1rya, resolution 1.30Å" /> | ||
'''Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG'''<br /> | '''Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG'''<br /> | ||
==Overview== | ==Overview== | ||
| - | GDP-mannose glycosyl hydrolase (GDPMH) catalyzes the hydrolysis of | + | 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== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Amzel, L | + | [[Category: Amzel, L M.]] |
| - | [[Category: Bianchet, M | + | [[Category: Bianchet, M A.]] |
| - | [[Category: Gabelli, S | + | [[Category: Gabelli, S B.]] |
| - | [[Category: Legler, P | + | [[Category: Legler, P M.]] |
| - | [[Category: Mildvan, A | + | [[Category: Mildvan, A S.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: GDP]] | [[Category: GDP]] | ||
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[[Category: nudix mg-complex]] | [[Category: nudix mg-complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:51 2008'' |
Revision as of 12:55, 21 February 2008
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Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG
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.
About this Structure
1RYA is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure and mechanism of GDP-mannose glycosyl hydrolase, a Nudix enzyme that cleaves at carbon instead of phosphorus., Gabelli SB, Bianchet MA, Azurmendi HF, Xia Z, Sarawat V, Mildvan AS, Amzel LM, Structure. 2004 Jun;12(6):927-35. PMID:15274914
Page seeded by OCA on Thu Feb 21 14:55:51 2008
Categories: Escherichia coli | Single protein | Amzel, L M. | Bianchet, M A. | Gabelli, S B. | Legler, P M. | Mildvan, A S. | CL | GDP | MG | TRS | Gdp-glucose | Gdp-mannose | Mannose | Nudix | Nudix mg-complex
