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1wd3
From Proteopedia
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| - | [[Image:1wd3.gif|left|200px]] | + | [[Image:1wd3.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of arabinofuranosidase''' | + | {{Structure |
| + | |PDB= 1wd3 |SIZE=350|CAPTION= <scene name='initialview01'>1wd3</scene>, resolution 1.75Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of arabinofuranosidase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1WD3 is a [ | + | 1WD3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_kawachii Aspergillus kawachii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WD3 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose., Miyanaga A, Koseki T, Matsuzawa H, Wakagi T, Shoun H, Fushinobu S, J Biol Chem. 2004 Oct 22;279(43):44907-14. Epub 2004 Aug 3. PMID:[http:// | + | Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose., Miyanaga A, Koseki T, Matsuzawa H, Wakagi T, Shoun H, Fushinobu S, J Biol Chem. 2004 Oct 22;279(43):44907-14. Epub 2004 Aug 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15292273 15292273] |
[[Category: Alpha-N-arabinofuranosidase]] | [[Category: Alpha-N-arabinofuranosidase]] | ||
[[Category: Aspergillus kawachii]] | [[Category: Aspergillus kawachii]] | ||
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[[Category: beta-trefoil]] | [[Category: beta-trefoil]] | ||
| - | ''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 14:55:31 2008'' |
Revision as of 12:55, 20 March 2008
| |||||||
| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Alpha-N-arabinofuranosidase, with EC number 3.2.1.55 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of arabinofuranosidase
Overview
As the first known structures of a glycoside hydrolase family 54 (GH54) enzyme, we determined the crystal structures of free and arabinose-complex forms of Aspergillus kawachii IFO4308 alpha-l-arabinofuranosidase (AkAbfB). AkAbfB comprises two domains: a catalytic domain and an arabinose-binding domain (ABD). The catalytic domain has a beta-sandwich fold similar to those of clan-B glycoside hydrolases. ABD has a beta-trefoil fold similar to that of carbohydrate-binding module (CBM) family 13. However, ABD shows a number of characteristics distinctive from those of CBM family 13, suggesting that it could be classified into a new CBM family. In the arabinose-complex structure, one of three arabinofuranose molecules is bound to the catalytic domain through many interactions. Interestingly, a disulfide bond formed between two adjacent cysteine residues recognized the arabinofuranose molecule in the active site. From the location of this arabinofuranose and the results of a mutational study, the nucleophile and acid/base residues were determined to be Glu(221) and Asp(297), respectively. The other two arabinofuranose molecules are bound to ABD. The O-1 atoms of the two arabinofuranose molecules bound at ABD are both pointed toward the solvent, indicating that these sites can both accommodate an arabinofuranose side-chain moiety linked to decorated arabinoxylans.
About this Structure
1WD3 is a Single protein structure of sequence from Aspergillus kawachii. Full crystallographic information is available from OCA.
Reference
Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose., Miyanaga A, Koseki T, Matsuzawa H, Wakagi T, Shoun H, Fushinobu S, J Biol Chem. 2004 Oct 22;279(43):44907-14. Epub 2004 Aug 3. PMID:15292273
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