1uwt
From Proteopedia
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|PDB= 1uwt |SIZE=350|CAPTION= <scene name='initialview01'>1uwt</scene>, resolution 1.95Å | |PDB= 1uwt |SIZE=350|CAPTION= <scene name='initialview01'>1uwt</scene>, resolution 1.95Å | ||
|SITE= <scene name='pdbsite=AC1:Gtl+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gtl+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GTL:(2E,3R,4R,5R,6S)-3,4,5-TRIHYDROXY-6-(HYDROXYMETHYL)-2-PIPERIDINONE'>GTL</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uwt OCA], [http://www.ebi.ac.uk/pdbsum/1uwt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uwt RCSB]</span> | ||
}} | }} | ||
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[[Category: Rossi, M.]] | [[Category: Rossi, M.]] | ||
[[Category: Vasella, A.]] | [[Category: Vasella, A.]] | ||
| - | + | [[Category: archaeon d-galactohydroximo-1,5-lactam]] | |
| - | + | ||
| - | + | ||
| - | [[Category: archaeon d-galactohydroximo-1]] | + | |
[[Category: family 1]] | [[Category: family 1]] | ||
[[Category: glycoside hydrolase]] | [[Category: glycoside hydrolase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:16:23 2008'' |
Revision as of 21:16, 30 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Beta-galactosidase, with EC number 3.2.1.23 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS IN COMPLEX WITH D-GALACTOHYDROXIMO-1,5-LACTAM
Overview
Transition-state mimicry is increasingly important both to understand enzyme mechanism and to direct the synthesis of putative therapeutic agents. X-ray crystallography is able to provide vital information on the interactions between an enzyme and the potential inhibitor. Here we report the structures, at approximately 2 A resolution, of a family GH1 beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus, in complex with both covalently (derived from 2-fluoro-glycosides) and noncovalently (hydroximolactam) bound inhibitors. The enzyme has broad specificity, accommodating both gluco- and galacto-configured substrates, and the crystallographic data demonstrate that the only difference in the way these ligands bind lies in the interactions between Gln18, Glu432, and Trp433, and the hydroxyl group at the O3 and O4 positions. Inhibition by the differently configured ligands was also shown to be extremely similar, with K(i) values of 1.04 and 1.08 microM for the gluco and galacto epimers, respectively. The noncovalently bound inhibitors have a trigonal anomeric carbon, adopt a (4)H(3) (half-chair) conformation, and an interaction is formed between O2 and the catalytic nucleophile, all of which contribute to (partial) mimicry of the oxocarbenium-ion-like transition state. The inhibition of the beta-glycosidase from S. solfataricus by hydroximolactams is discussed in light of the emerging work on family GH1 glycosidase inhibition by a spectrum of putative transition-state mimics.
About this Structure
1UWT is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
Structural studies of the beta-glycosidase from Sulfolobus solfataricus in complex with covalently and noncovalently bound inhibitors., Gloster TM, Roberts S, Ducros VM, Perugino G, Rossi M, Hoos R, Moracci M, Vasella A, Davies GJ, Biochemistry. 2004 May 25;43(20):6101-9. PMID:15147194
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