1e70: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1e70.gif|left|200px]] | [[Image:1e70.gif|left|200px]] | ||
'''2-F-GLUCOSYLATED MYROSINASE FROM SINAPIS ALBA''' | {{Structure | ||
|PDB= 1e70 |SIZE=350|CAPTION= <scene name='initialview01'>1e70</scene>, resolution 1.65Å | |||
|SITE= <scene name='pdbsite=ACT:Glc+Binding+Subsite+Of+Active+Site'>ACT</scene>, <scene name='pdbsite=ASC:Ascorbate+Binding+Site'>ASC</scene> and <scene name='pdbsite=ZNB:Zn+Binding+Site+Together+w.+The+Symmetry-Related+Equivalents'>ZNB</scene> | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=G2F:2-DEOXY-2FLUORO-GLUCOSE'>G2F</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_3.2.1.147 Transferred entry: 3.2.1.147], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.3.1 3.2.3.1] | |||
|GENE= | |||
}} | |||
'''2-F-GLUCOSYLATED MYROSINASE FROM SINAPIS ALBA''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1E70 is a [ | 1E70 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Sinapis_alba Sinapis alba]. This structure supersedes the now removed PDB entry 2MYR. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E70 OCA]. | ||
==Reference== | ==Reference== | ||
High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base., Burmeister WP, Cottaz S, Rollin P, Vasella A, Henrissat B, J Biol Chem. 2000 Dec 15;275(50):39385-93. PMID:[http:// | High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base., Burmeister WP, Cottaz S, Rollin P, Vasella A, Henrissat B, J Biol Chem. 2000 Dec 15;275(50):39385-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10978344 10978344] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Sinapis alba]] | [[Category: Sinapis alba]] | ||
| Line 26: | Line 35: | ||
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:50:49 2008'' | ||
Revision as of 11:50, 20 March 2008
| |||||||
| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , , , and | ||||||
| Activity: | Transferred entry: 3.2.1.147, with EC number 3.2.3.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
2-F-GLUCOSYLATED MYROSINASE FROM SINAPIS ALBA
OverviewOverview
Myrosinase, an S-glycosidase, hydrolyzes plant anionic 1-thio-beta-d-glucosides (glucosinolates) considered part of the plant defense system. Although O-glycosidases are ubiquitous, myrosinase is the only known S-glycosidase. Its active site is very similar to that of retaining O-glycosidases, but one of the catalytic residues in O-glycosidases, a carboxylate residue functioning as the general base, is replaced by a glutamine residue. Myrosinase is strongly activated by ascorbic acid. Several binary and ternary complexes of myrosinase with different transition state analogues and ascorbic acid have been analyzed at high resolution by x-ray crystallography along with a 2-deoxy-2-fluoro-glucosyl enzyme intermediate. One of the inhibitors, d-gluconhydroximo-1,5-lactam, binds simultaneously with a sulfate ion to form a mimic of the enzyme-substrate complex. Ascorbate binds to a site distinct from the glucose binding site but overlapping with the aglycon binding site, suggesting that activation occurs at the second step of catalysis, i.e. hydrolysis of the glycosyl enzyme. A water molecule is placed perfectly for activation by ascorbate and for nucleophilic attack on the covalently trapped 2-fluoro-glucosyl-moiety. Activation of the hydrolysis of the glucosyl enzyme intermediate is further evidenced by the observation that ascorbate enhances the rate of reactivation of the 2-fluoro-glycosyl enzyme, leading to the conclusion that ascorbic acid substitutes for the catalytic base in myrosinase.
About this StructureAbout this Structure
1E70 is a Protein complex structure of sequences from Sinapis alba. This structure supersedes the now removed PDB entry 2MYR. Full crystallographic information is available from OCA.
ReferenceReference
High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base., Burmeister WP, Cottaz S, Rollin P, Vasella A, Henrissat B, J Biol Chem. 2000 Dec 15;275(50):39385-93. PMID:10978344
Page seeded by OCA on Thu Mar 20 10:50:49 2008