1ahp: Difference between revisions

Revision as of 16:52, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ahp.png

Template:STRUCTURE 1ahp

OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASEOLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE

Template:ABSTRACT PUBMED 9145112

About this StructureAbout this Structure

1AHP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase., O'Reilly M, Watson KA, Schinzel R, Palm D, Johnson LN, Nat Struct Biol. 1997 May;4(5):405-12. PMID:9145112

Page seeded by OCA on Mon Jun 30 16:52:34 2008

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-'''OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE'''
+===OLIGOSACCHARIDE SUBSTRATE BINDING IN ESCHERICHIA COLI MALTODEXTRIN PHSPHORYLASE===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9145112}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9145112 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9145112}}
 ==About this Structure==
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 [[Category: Stacking]]
 [[Category: Substrate]]
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