rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
5
|
pubmed:dateCreated |
1997-5-28
|
pubmed:abstractText |
The crystal structure of E. coli maltodextrin phosphorylase co-crystallized with an oligosaccharide has been solved at 3.0 A resolution, providing the first structure of an oligosaccharide bound at the catalytic site of an alpha-glucan phosphorylase. An induced fit mechanism brings together two domains across the catalytic site tunnel. A stacking interaction between the glucosyl residue and the aromatic group of a tyrosine residue at a sub-site remote (8 A) from the catalytic site provides a key element in substrate recognition; mutation of this residue to Ala decreases the Kcat/Km by 10(4). Extrapolation of the results to substrate binding across the site of attack by phosphorolysis indicates a likely alteration in the glycosidic torsion angles from their preferred values, an alteration that appears to be important for the catalytic mechanism.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
1072-8368
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
4
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
405-12
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:9145112-Crystallization,
pubmed-meshheading:9145112-Crystallography, X-Ray,
pubmed-meshheading:9145112-Escherichia coli,
pubmed-meshheading:9145112-Glucans,
pubmed-meshheading:9145112-Glucosyltransferases,
pubmed-meshheading:9145112-Kinetics,
pubmed-meshheading:9145112-Models, Molecular,
pubmed-meshheading:9145112-Oligosaccharides,
pubmed-meshheading:9145112-Protein Binding,
pubmed-meshheading:9145112-Protein Conformation,
pubmed-meshheading:9145112-Tyrosine
|
pubmed:year |
1997
|
pubmed:articleTitle |
Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase.
|
pubmed:affiliation |
Laboratory of Molecular Biophysics, University of Oxford.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|