1qw8: Difference between revisions

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[[Image:1qw8.jpg|left|200px]]<br /><applet load="1qw8" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1qw8.jpg|left|200px]]
caption="1qw8, resolution 1.80&Aring;" />
 
'''Crystal structure of a family 51 alpha-L-arabinofuranosidase in complex with Ara-alpha(1,3)-Xyl'''<br />
{{Structure
|PDB= 1qw8 |SIZE=350|CAPTION= <scene name='initialview01'>1qw8</scene>, resolution 1.80&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=KHO:4-(3,4-DIHYDROXY-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-2-YLOXY)-TETRAHYDRO-PYRAN-2,3,5-TRIOL'>KHO</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-N-arabinofuranosidase Alpha-N-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55]
|GENE= ABFA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])
}}
 
'''Crystal structure of a family 51 alpha-L-arabinofuranosidase in complex with Ara-alpha(1,3)-Xyl'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1QW8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=KHO:'>KHO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alpha-N-arabinofuranosidase Alpha-N-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QW8 OCA].  
1QW8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QW8 OCA].  


==Reference==
==Reference==
Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase., Hovel K, Shallom D, Niefind K, Belakhov V, Shoham G, Baasov T, Shoham Y, Schomburg D, EMBO J. 2003 Oct 1;22(19):4922-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14517232 14517232]
Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase., Hovel K, Shallom D, Niefind K, Belakhov V, Shoham G, Baasov T, Shoham Y, Schomburg D, EMBO J. 2003 Oct 1;22(19):4922-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14517232 14517232]
[[Category: Alpha-N-arabinofuranosidase]]
[[Category: Alpha-N-arabinofuranosidase]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: hydrolase]]
[[Category: hydrolase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:19 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:43:33 2008''

Revision as of 14:43, 20 March 2008

File:1qw8.jpg


PDB ID 1qw8

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands:
Gene: ABFA (Geobacillus stearothermophilus)
Activity: Alpha-N-arabinofuranosidase, with EC number 3.2.1.55
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a family 51 alpha-L-arabinofuranosidase in complex with Ara-alpha(1,3)-Xyl


OverviewOverview

High-resolution crystal structures of alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycosidase, are described. The enzyme is a hexamer, and each monomer is organized into two domains: a (beta/alpha)8-barrel and a 12-stranded beta sandwich with jelly-roll topology. The structures of the Michaelis complexes with natural and synthetic substrates, and of the transient covalent arabinofuranosyl-enzyme intermediate represent two stable states in the double displacement mechanism, and allow thorough examination of the catalytic mechanism. The arabinofuranose sugar is tightly bound and distorted by an extensive network of hydrogen bonds. The two catalytic residues are 4.7 A apart, and together with other conserved residues contribute to the stabilization of the oxocarbenium ion-like transition state via charge delocalization and specific protein-substrate interactions. The enzyme is an anti-protonator, and a 1.7 A electrophilic migration of the anomeric carbon takes place during the hydrolysis.

About this StructureAbout this Structure

1QW8 is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase., Hovel K, Shallom D, Niefind K, Belakhov V, Shoham G, Baasov T, Shoham Y, Schomburg D, EMBO J. 2003 Oct 1;22(19):4922-32. PMID:14517232

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