1rya: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1rya |SIZE=350|CAPTION= <scene name='initialview01'>1rya</scene>, resolution 1.30Å | |PDB= 1rya |SIZE=350|CAPTION= <scene name='initialview01'>1rya</scene>, resolution 1.30Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDP:GUANOSINE-5'-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> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= NUDD, WCAH, GMM, B2051 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= NUDD, WCAH, GMM, B2051 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|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> | |||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Legler, P M.]] | [[Category: Legler, P M.]] | ||
[[Category: Mildvan, A S.]] | [[Category: Mildvan, A S.]] | ||
[[Category: gdp-glucose]] | [[Category: gdp-glucose]] | ||
[[Category: gdp-mannose]] | [[Category: gdp-mannose]] | ||
| Line 37: | Line 36: | ||
[[Category: nudix mg-complex]] | [[Category: nudix mg-complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:34:41 2008'' | ||
Revision as of 23:34, 30 March 2008
| |||||||
| , resolution 1.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | NUDD, WCAH, GMM, B2051 (Escherichia coli) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG
OverviewOverview
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 StructureAbout this Structure
1RYA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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 Sun Mar 30 23:34:41 2008