1rya

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{{STRUCTURE_1rya| PDB=1rya | SCENE= }}
{{STRUCTURE_1rya| PDB=1rya | SCENE= }}
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'''Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG'''
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===Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15274914 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15274914}}
==About this Structure==
==About this Structure==
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[[Category: Nudix]]
[[Category: Nudix]]
[[Category: Nudix mg-complex]]
[[Category: Nudix mg-complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:03:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:08:54 2008''

Revision as of 10:08, 28 July 2008

Image:1rya.png

Template:STRUCTURE 1rya

Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG

Template:ABSTRACT PUBMED 15274914

About this Structure

1RYA is a Single protein structure of sequence from Escherichia coli. 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

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