1pz3
From Proteopedia
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| - | [[Image:1pz3.jpg|left|200px]] | + | [[Image:1pz3.jpg|left|200px]] |
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| - | '''Crystal structure of a family 51 (GH51) alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T6''' | + | {{Structure |
| + | |PDB= 1pz3 |SIZE=350|CAPTION= <scene name='initialview01'>1pz3</scene>, resolution 1.75Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</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 (GH51) alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T6''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PZ3 is a [ | + | 1PZ3 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=1PZ3 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:// | + | 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: beta-alpha8-barrel]] | [[Category: beta-alpha8-barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:30:53 2008'' |
Revision as of 11:30, 20 March 2008
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| , resolution 1.75Å | |||||||
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| 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 (GH51) alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T6
Overview
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 Structure
1PZ3 is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
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:14517232
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