1iin: Difference between revisions
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=UPG:URIDINE-5'-DIPHOSPHATE-GLUCOSE'>UPG</scene> | |LIGAND= <scene name='pdbligand=UPG:URIDINE-5'-DIPHOSPHATE-GLUCOSE'>UPG</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Glucose-1-phosphate_thymidylyltransferase Glucose-1-phosphate thymidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-1-phosphate_thymidylyltransferase Glucose-1-phosphate thymidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1iim|1IIM]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iin OCA], [http://www.ebi.ac.uk/pdbsum/1iin PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iin RCSB]</span> | |||
}} | }} | ||
| Line 31: | Line 34: | ||
[[Category: Rajashankar, K R.]] | [[Category: Rajashankar, K R.]] | ||
[[Category: Thorson, J S.]] | [[Category: Thorson, J S.]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:20:21 2008'' | ||
Revision as of 21:20, 30 March 2008
| |||||||
| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glucose-1-phosphate thymidylyltransferase, with EC number 2.7.7.24 | ||||||
| Related: | 1IIM
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
thymidylyltransferase complexed with UDP-glucose
OverviewOverview
Metabolite glycosylation is affected by three classes of enzymes: nucleotidylyltransferases, which activate sugars as nucleotide diphospho-derivatives, intermediate sugar-modifying enzymes and glycosyltransferases, which transfer the final derivatized activated sugars to aglycon substrates. One of the first crystal structures of an enzyme responsible for the first step in this cascade, alpha-D-glucopyranosyl phosphate thymidylyltransferase (Ep) from Salmonella, in complex with product (UDP-Glc) and substrate (dTTP) is reported at 2.0 A and 2.1 A resolution, respectively. These structures, in conjunction with the kinetic characterization of Ep, clarify the catalytic mechanism of this important enzyme class. Structure-based engineering of Ep produced modified enzymes capable of utilizing 'unnatural' sugar phosphates not accepted by wild type Ep. The demonstrated ability to alter nucleotidylyltransferase specificity by design is an integral component of in vitro glycosylation systems developed for the production of diverse glycorandomized libraries.
About this StructureAbout this Structure
1IIN is a Single protein structure of sequence from Salmonella enterica. Full crystallographic information is available from OCA.
ReferenceReference
Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization., Barton WA, Lesniak J, Biggins JB, Jeffrey PD, Jiang J, Rajashankar KR, Thorson JS, Nikolov DB, Nat Struct Biol. 2001 Jun;8(6):545-51. PMID:11373625
Page seeded by OCA on Sun Mar 30 21:20:21 2008