1ahp
From Proteopedia
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|PDB= 1ahp |SIZE=350|CAPTION= <scene name='initialview01'>1ahp</scene>, resolution 3.0Å | |PDB= 1ahp |SIZE=350|CAPTION= <scene name='initialview01'>1ahp</scene>, resolution 3.0Å | ||
|SITE= <scene name='pdbsite=1:Catalytic+Site+Is+Located+At+The+Base+Of+A+Cleft+Between+...'>1</scene> | |SITE= <scene name='pdbsite=1:Catalytic+Site+Is+Located+At+The+Base+Of+A+Cleft+Between+...'>1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ahp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahp OCA], [http://www.ebi.ac.uk/pdbsum/1ahp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ahp RCSB]</span> | ||
}} | }} | ||
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[[Category: Schinzel, R.]] | [[Category: Schinzel, R.]] | ||
[[Category: Watson, K A.]] | [[Category: Watson, K A.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: MAL]] | ||
| - | [[Category: PLP]] | ||
| - | [[Category: SO4]] | ||
[[Category: ecoli]] | [[Category: ecoli]] | ||
[[Category: induced-fit]] | [[Category: induced-fit]] | ||
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[[Category: substrate]] | [[Category: substrate]] | ||
| - | ''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 18:40:25 2008'' |
Revision as of 15:40, 30 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Phosphorylase, with EC number 2.4.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1AHP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Sun Mar 30 18:40:25 2008
