2bgm
From Proteopedia
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| - | [[Image:2bgm.gif|left|200px]]<br /> | + | [[Image:2bgm.gif|left|200px]]<br /><applet load="2bgm" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2bgm" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2bgm, resolution 2.0Å" /> | caption="2bgm, resolution 2.0Å" /> | ||
'''X-RAY STRUCTURE OF TERNARY-SECOISOLARICIRESINOL DEHYDROGENASE'''<br /> | '''X-RAY STRUCTURE OF TERNARY-SECOISOLARICIRESINOL DEHYDROGENASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BGM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Podophyllum_peltatum Podophyllum peltatum] with NAJ and MAX as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 2BGM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Podophyllum_peltatum Podophyllum peltatum] with NAJ and MAX as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Max Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BGM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:46:07 2007'' |
Revision as of 16:36, 18 December 2007
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X-RAY STRUCTURE OF TERNARY-SECOISOLARICIRESINOL DEHYDROGENASE
Overview
(-)-Matairesinol is a central biosynthetic intermediate to numerous, 8-8'-lignans, including the antiviral agent podophyllotoxin in Podophyllum, species and its semi-synthetic anticancer derivatives teniposide, etoposide, and Etopophos. It is formed by action of an enantiospecific, secoisolariciresinol dehydrogenase, an NAD(H)-dependent oxidoreductase, that catalyzes the conversion of (-)-secoisolariciresinol. Matairesinol is, also a plant-derived precursor of the cancer-preventative "mammalian", lignan or "phytoestrogen" enterolactone, formed in the gut following, ingestion of high fiber dietary foodstuffs, for example. Additionally, secoisolariciresinol dehydrogenase is involved in pathways to important, plant defense molecules, such as plicatic acid in the western red cedar, (Thuja plicata) heartwood. To understand the molecular and enantiospecific, basis of Podophyllum secoisolariciresinol dehydrogenase, crystal, structures of the apo-form and binary/ternary complexes were determined at, 1.6, 2.8, and 2.0 angstrom resolution, respectively. The enzyme is a, homotetramer, consisting of an alpha/beta single domain monomer containing, seven parallel beta-strands flanked by eight alpha-helices on both sides., Its overall monomeric structure is similar to that of NAD(H)-dependent, short-chain dehydrogenases/reductases, with a conserved Asp47 forming a, hydrogen bond with both hydroxyl groups of the adenine ribose of NAD(H), and thus specificity toward NAD(H) instead of NADP(H). The highly, conserved catalytic triad (Ser153, Tyr167, and Lys171) is adjacent to both, NAD(+) and substrate molecules, where Tyr167 functions as a general base., Following analysis of high resolution structures of the apo-form and two, complex forms, the molecular basis for both the enantio-specificity and, the reaction mechanism of secoisolariciresinol dehydrogenase is discussed, and compared with that of pinoresinol-lariciresinol reductase.
About this Structure
2BGM is a Single protein structure of sequence from Podophyllum peltatum with NAJ and MAX as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structures of apo-form and binary/ternary complexes of Podophyllum secoisolariciresinol dehydrogenase, an enzyme involved in formation of health-protecting and plant defense lignans., Youn B, Moinuddin SG, Davin LB, Lewis NG, Kang C, J Biol Chem. 2005 Apr 1;280(13):12917-26. Epub 2005 Jan 13. PMID:15653677
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