2g8s

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[[Image:2g8s.gif|left|200px]]
[[Image:2g8s.gif|left|200px]]
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{{Structure
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|GENE= yliI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_2g8s| PDB=2g8s | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g8s OCA], [http://www.ebi.ac.uk/pdbsum/2g8s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2g8s RCSB]</span>
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'''Crystal structure of the soluble Aldose sugar dehydrogenase (Asd) from Escherichia coli in the apo-form'''
'''Crystal structure of the soluble Aldose sugar dehydrogenase (Asd) from Escherichia coli in the apo-form'''
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[[Category: Southall, S M.]]
[[Category: Southall, S M.]]
[[Category: 6 bladed beta-propellor]]
[[Category: 6 bladed beta-propellor]]
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[[Category: pyrolloquinoline quinone (pqq)]]
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[[Category: Quinoprotein]]
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[[Category: quinoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:49:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:13:23 2008''
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Revision as of 01:49, 4 May 2008

Template:STRUCTURE 2g8s

Crystal structure of the soluble Aldose sugar dehydrogenase (Asd) from Escherichia coli in the apo-form


Overview

A water-soluble aldose sugar dehydrogenase (Asd) has been purified for the first time from Escherichia coli. The enzyme is able to act upon a broad range of aldose sugars, encompassing hexoses, pentoses, disaccharides, and trisaccharides, and is able to oxidize glucose to gluconolactone with subsequent hydrolysis to gluconic acid. The enzyme shows the ability to bind pyrroloquinoline quinone (PQQ) in the presence of Ca2+ in a manner that is proportional to its catalytic activity. The x-ray structure has been determined in the apo-form and as the PQQ-bound active holoenzyme. The beta-propeller fold of this protein is conserved between E. coli Asd and Acinetobacter calcoaceticus soluble glucose dehydrogenase (sGdh), with major structural differences lying in loop and surface-exposed regions. Many of the residues involved in binding the cofactor are conserved between the two enzymes, but significant differences exist in residues likely to contact substrates. PQQ is bound in a large cleft in the protein surface and is uniquely solvent-accessible compared with other PQQ enzymes. The exposed and charged nature of the active site and the activity profile of this enzyme indicate possible factors that underlie a low affinity for glucose but generic broad substrate specificity for aldose sugars. These structural and catalytic properties of the enzymes have led us to propose that E. coli Asd provides a prototype structure for a new subgroup of PQQ-dependent soluble dehydrogenases that is distinct from the A. calcoaceticus sGdh subgroup.

About this Structure

2G8S is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Soluble aldose sugar dehydrogenase from Escherichia coli: a highly exposed active site conferring broad substrate specificity., Southall SM, Doel JJ, Richardson DJ, Oubrie A, J Biol Chem. 2006 Oct 13;281(41):30650-9. Epub 2006 Jul 24. PMID:16864586 Page seeded by OCA on Sun May 4 04:49:45 2008

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