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| | {{STRUCTURE_2hor| PDB=2hor | SCENE= }} | | {{STRUCTURE_2hor| PDB=2hor | SCENE= }} |
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| - | '''Crystal structure of alliinase from garlic- apo form'''
| + | ===Crystal structure of alliinase from garlic- apo form=== |
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| - | ==Overview==
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| - | Alliinase (alliin lyase EC 4.4.1.4), a PLP-dependent alpha, beta-eliminating lyase, constitutes one of the major protein components of garlic (Alliium sativum L.) bulbs. The enzyme is a homodimeric glycoprotein and catalyzes the conversion of a specific non-protein sulfur-containing amino acid alliin ((+S)-allyl-L-cysteine sulfoxide) to allicin (diallyl thiosulfinate, the well known biologically active component of freshly crushed garlic), pyruvate and ammonia. The enzyme was crystallized in the presence of (+S)-allyl-L-cysteine, forming dendrite-like monoclinic crystals. In addition, intentionally produced apo-enzyme was crystallized in tetragonal form. These structures of alliinase with associated glycans were resolved to 1.4 A and 1.61 A by molecular replacement. Branched hexasaccharide chains N-linked to Asn146 and trisaccharide chains N-linked to Asn328 are seen. The structure of hexasaccharide was found similar to "short chain complex vacuole type" oligosaccharide most commonly seen in plant glycoproteins. An unexpected state of the enzyme active site has been observed in the present structure. The electron density in the region of the cofactor made it possible to identify the cofactor moiety as aminoacrylate intermediate covalently bound to the PLP cofactor. It was found in the present structure to be stabilized by large number of interactions with surrounding protein residues. Moreover, the existence of the expected internal aldimine bond between the epsilon-amino group of Lys251 and the aldehyde of the PLP is ruled out on the basis of a distinct separation of electron density of Lys251. The structure of the active site cavity in the apo-form is nearly identical to that seen in the holo-form, with two sulfate ions, an acetate and several water molecules from crystallization conditions that replace and mimic the PLP cofactor.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17174334}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17174334 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17174334}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Plant enzyme]] | | [[Category: Plant enzyme]] |
| | [[Category: Pyridoxal-5'-phosphate]] | | [[Category: Pyridoxal-5'-phosphate]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:31:35 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:43:19 2008'' |
Revision as of 11:43, 29 July 2008
Template:STRUCTURE 2hor
Crystal structure of alliinase from garlic- apo form
Template:ABSTRACT PUBMED 17174334
About this Structure
2HOR is a Single protein structure of sequence from Allium sativum. Full crystallographic information is available from OCA.
Reference
Two structures of alliinase from Alliium sativum L.: apo form and ternary complex with aminoacrylate reaction intermediate covalently bound to the PLP cofactor., Shimon LJ, Rabinkov A, Shin I, Miron T, Mirelman D, Wilchek M, Frolow F, J Mol Biol. 2007 Feb 16;366(2):611-25. Epub 2006 Nov 14. PMID:17174334
Page seeded by OCA on Tue Jul 29 14:43:19 2008
