2ac1
From Proteopedia
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|PDB= 2ac1 |SIZE=350|CAPTION= <scene name='initialview01'>2ac1</scene>, resolution 2.15Å | |PDB= 2ac1 |SIZE=350|CAPTION= <scene name='initialview01'>2ac1</scene>, resolution 2.15Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-fructofuranosidase Beta-fructofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.26 3.2.1.26] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-fructofuranosidase Beta-fructofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.26 3.2.1.26] </span> |
|GENE= At3g13790 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]) | |GENE= At3g13790 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ac1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ac1 OCA], [http://www.ebi.ac.uk/pdbsum/2ac1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ac1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Roy, K Le.]] | [[Category: Roy, K Le.]] | ||
[[Category: Verhaest, M.]] | [[Category: Verhaest, M.]] | ||
- | [[Category: GOL]] | ||
- | [[Category: NAG]] | ||
[[Category: five fold beta propeller]] | [[Category: five fold beta propeller]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:50:43 2008'' |
Revision as of 22:50, 30 March 2008
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, resolution 2.15Å | |||||||
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Ligands: | , , | ||||||
Gene: | At3g13790 (Arabidopsis thaliana) | ||||||
Activity: | Beta-fructofuranosidase, with EC number 3.2.1.26 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of a cell-wall invertase from Arabidopsis thaliana
Overview
Cell-wall invertases play crucial roles during plant development. They hydrolyse sucrose into its fructose and glucose subunits by cleavage of the alpha1-beta2 glycosidic bond. Here, the structure of the Arabidopsis thaliana cell-wall invertase 1 (AtcwINV1; gene accession code At3g13790) is described at a resolution of 2.15 A. The structure comprises an N-terminal fivefold beta-propeller domain followed by a C-terminal domain formed by two beta-sheets. The active site is positioned in the fivefold beta-propeller domain, containing the nucleophile Asp23 and the acid/base catalyst Glu203 of the double-displacement enzymatic reaction. The function of the C-terminal domain remains unknown. Unlike in other GH 32 family enzyme structures known to date, in AtcwINV1 the cleft formed between both domains is blocked by Asn299-linked carbohydrates. A preliminary site-directed mutagenesis experiment (Asn299Asp) removed the glycosyl chain but did not alter the activity profile of the enzyme.
About this Structure
2AC1 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
X-ray diffraction structure of a cell-wall invertase from Arabidopsis thaliana., Verhaest M, Lammens W, Le Roy K, De Coninck B, De Ranter CJ, Van Laere A, Van den Ende W, Rabijns A, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1555-63. Epub 2006, Nov 23. PMID:17139091
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