1rya

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[[Image:1rya.jpg|left|200px]]
[[Image:1rya.jpg|left|200px]]
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{{Structure
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|PDB= 1rya |SIZE=350|CAPTION= <scene name='initialview01'>1rya</scene>, resolution 1.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1rya", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|GENE= NUDD, WCAH, GMM, B2051 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1rya| PDB=1rya | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rya OCA], [http://www.ebi.ac.uk/pdbsum/1rya PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rya RCSB]</span>
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'''Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG'''
'''Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG'''
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[[Category: Legler, P M.]]
[[Category: Legler, P M.]]
[[Category: Mildvan, A S.]]
[[Category: Mildvan, A S.]]
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[[Category: gdp-glucose]]
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[[Category: Gdp-glucose]]
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[[Category: gdp-mannose]]
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[[Category: Gdp-mannose]]
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[[Category: mannose]]
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[[Category: Mannose]]
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[[Category: nudix]]
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[[Category: Nudix]]
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[[Category: nudix mg-complex]]
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[[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 Sun Mar 30 23:34:41 2008''
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Revision as of 05:03, 3 May 2008

Image:1rya.jpg

Template:STRUCTURE 1rya

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. 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 Sat May 3 08:03:24 2008

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