2bgh
From Proteopedia
(New page: 200px<br /><applet load="2bgh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bgh, resolution 2.60Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:2bgh.gif|left|200px]]<br /><applet load="2bgh" size=" | + | [[Image:2bgh.gif|left|200px]]<br /><applet load="2bgh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bgh, resolution 2.60Å" /> | caption="2bgh, resolution 2.60Å" /> | ||
'''CRYSTAL STRUCTURE OF VINORINE SYNTHASE'''<br /> | '''CRYSTAL STRUCTURE OF VINORINE SYNTHASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Vinorine synthase is an acetyltransferase that occupies a central role in | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2BGH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rauvolfia_serpentina Rauvolfia serpentina]. Active as [http://en.wikipedia.org/wiki/Vinorine_synthase Vinorine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.160 2.3.1.160] Full crystallographic information is available from [http:// | + | 2BGH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rauvolfia_serpentina Rauvolfia serpentina]. Active as [http://en.wikipedia.org/wiki/Vinorine_synthase Vinorine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.160 2.3.1.160] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BGH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: vs]] | [[Category: vs]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:35 2008'' |
Revision as of 14:37, 21 February 2008
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CRYSTAL STRUCTURE OF VINORINE SYNTHASE
Overview
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.
About this Structure
2BGH is a Single protein structure of sequence from Rauvolfia serpentina. Active as Vinorine synthase, with EC number 2.3.1.160 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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