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| | {{STRUCTURE_2bgh| PDB=2bgh | SCENE= }} | | {{STRUCTURE_2bgh| PDB=2bgh | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF VINORINE SYNTHASE'''
| + | ===CRYSTAL STRUCTURE OF VINORINE SYNTHASE=== |
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| - | ==Overview==
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| - | Vinorine synthase is an acetyltransferase that occupies a central role in the biosynthesis of the antiarrhythmic monoterpenoid indole alkaloid ajmaline in the plant Rauvolfia. Vinorine synthase belongs to the benzylalcohol acetyl-, anthocyanin-O-hydroxy-cinnamoyl-, anthranilate-N-hydroxy-cinnamoyl/benzoyl-, deacetylvindoline acetyltransferase (BAHD) enzyme superfamily, members of which are involved in the biosynthesis of several important drugs, such as morphine, Taxol, or vindoline, a precursor of the anti-cancer drugs vincaleucoblastine and vincristine. The x-ray structure of vinorine synthase is described at 2.6-angstrom resolution. Despite low sequence identity, the two-domain structure of vinorine synthase shows surprising similarity with structures of several CoA-dependent acyltransferases such as dihydrolipoyl transacetylase, polyketide-associated protein A5, and carnitine acetyltransferase. All conserved residues typical for the BAHD family are found in domain 1. His160 of the HXXXD motif functions as a general base during catalysis. It is located in the center of the reaction channel at the interface of both domains and is accessible from both sides. The channel runs through the entire molecule, allowing the substrate and co-substrate to bind independently. Asp164 points away from the catalytic site and seems to be of structural rather than catalytic importance. Surprisingly, the DFGWG motif, which is indispensable for the catalyzed reaction and unique to the BAHD family, is located far away from the active site and seems to play only a structural role. Vinorine synthase represents the first solved protein structure of the BAHD superfamily.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15665331}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15665331 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15665331}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Transferase]] | | [[Category: Transferase]] |
| | [[Category: V]] | | [[Category: V]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:15:11 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:06:26 2008'' |
Revision as of 12:06, 29 July 2008
Template:STRUCTURE 2bgh
CRYSTAL STRUCTURE OF VINORINE SYNTHASE
Template:ABSTRACT PUBMED 15665331
About this Structure
2BGH is a Single protein structure of sequence from Rauvolfia serpentina. Full crystallographic information is available from OCA.
Reference
Crystal structure of vinorine synthase, the first representative of the BAHD superfamily., Ma X, Koepke J, Panjikar S, Fritzsch G, Stockigt J, J Biol Chem. 2005 Apr 8;280(14):13576-83. Epub 2005 Jan 22. PMID:15665331
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