1rya

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[[Image:1rya.jpg|left|200px]]<br /><applet load="1rya" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rya.jpg|left|200px]]
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caption="1rya, resolution 1.30&Aring;" />
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'''Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG'''<br />
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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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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|ACTIVITY=
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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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}}
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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==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1RYA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RYA OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15274914 15274914]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15274914 15274914]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: nudix mg-complex]]
[[Category: nudix mg-complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:57:52 2008''

Revision as of 11:57, 20 March 2008

Image:1rya.jpg


PDB ID 1rya

Drag the structure with the mouse to rotate
, resolution 1.30Å
Ligands: , , and
Gene: NUDD, WCAH, GMM, B2051 (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



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

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