2AC1
Crystal structure of a cell-wall invertase from Arabidopsis thaliana
Summary for 2AC1
| Entry DOI | 10.2210/pdb2ac1/pdb |
| Descriptor | invertase, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | five fold beta propeller, hydrolase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Cellular location | Secreted, extracellular space, apoplast (Probable): Q43866 |
| Total number of polymer chains | 1 |
| Total formula weight | 63722.53 |
| Authors | Verhaest, M.,Le Roy, K.,De Ranter, C.,Van Laere, A.,Van den Ende, W.,Rabijns, A. (deposition date: 2005-07-18, release date: 2006-08-29, Last modification date: 2024-10-30) |
| Primary citation | Verhaest, M.,Lammens, W.,Le Roy, K.,De Coninck, B.,De Ranter, C.J.,Van Laere, A.,Van den Ende, W.,Rabijns, A. X-ray diffraction structure of a cell-wall invertase from Arabidopsis thaliana. Acta Crystallogr.,Sect.D, 62:1555-1563, 2006 Cited by PubMed Abstract: 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. PubMed: 17139091DOI: 10.1107/S0907444906044489 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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