1r37
From Proteopedia
(New page: 200px<br /><applet load="1r37" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r37, resolution 2.30Å" /> '''Alcohol dehydrogenas...) |
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| - | [[Image:1r37.jpg|left|200px]]<br /><applet load="1r37" size=" | + | [[Image:1r37.jpg|left|200px]]<br /><applet load="1r37" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r37, resolution 2.30Å" /> | caption="1r37, resolution 2.30Å" /> | ||
'''Alcohol dehydrogenase from sulfolobus solfataricus complexed with NAD(H) and 2-ethoxyethanol'''<br /> | '''Alcohol dehydrogenase from sulfolobus solfataricus complexed with NAD(H) and 2-ethoxyethanol'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a ternary complex of the alcohol dehydrogenase | + | The crystal structure of a ternary complex of the alcohol dehydrogenase from the archaeon Sulfolobus solfataricus (SsADH) has been determined at 2.3 A. The asymmetric unit contains a dimer with a NADH and a 2-ethoxyethanol molecule bound to each subunit. The comparison with the apo structure of the enzyme reveals that this medium chain ADH undergoes a substantial conformational change in the apo-holo transition, accompanied by loop movements at the domain interface. The extent of domain closure is similar to that observed for the classical horse liver ADH, although some differences are found which can be related to the different oligomeric states of the enzymes. Compared to its apo form, the SsADH ternary complex shows a change in the ligation state of the active site zinc ion which is no longer bound to Glu69, providing additional evidence of the dynamic role played by the conserved glutamate residue in ADHs. In addition, the structure presented here allows the identification of the substrate site and hence of the residues that are important in the binding of both the substrate and the coenzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1R37 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with ZN, NAD and ETX as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Full crystallographic information is available from [http:// | + | 1R37 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=ETX:'>ETX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R37 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Giordano, A.]] | [[Category: Giordano, A.]] | ||
[[Category: Mazzarella, L.]] | [[Category: Mazzarella, L.]] | ||
| - | [[Category: Raia, C | + | [[Category: Raia, C A.]] |
[[Category: Rossi, M.]] | [[Category: Rossi, M.]] | ||
[[Category: Sica, F.]] | [[Category: Sica, F.]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:31 2008'' |
Revision as of 12:46, 21 February 2008
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Alcohol dehydrogenase from sulfolobus solfataricus complexed with NAD(H) and 2-ethoxyethanol
Overview
The crystal structure of a ternary complex of the alcohol dehydrogenase from the archaeon Sulfolobus solfataricus (SsADH) has been determined at 2.3 A. The asymmetric unit contains a dimer with a NADH and a 2-ethoxyethanol molecule bound to each subunit. The comparison with the apo structure of the enzyme reveals that this medium chain ADH undergoes a substantial conformational change in the apo-holo transition, accompanied by loop movements at the domain interface. The extent of domain closure is similar to that observed for the classical horse liver ADH, although some differences are found which can be related to the different oligomeric states of the enzymes. Compared to its apo form, the SsADH ternary complex shows a change in the ligation state of the active site zinc ion which is no longer bound to Glu69, providing additional evidence of the dynamic role played by the conserved glutamate residue in ADHs. In addition, the structure presented here allows the identification of the substrate site and hence of the residues that are important in the binding of both the substrate and the coenzyme.
About this Structure
1R37 is a Single protein structure of sequence from Sulfolobus solfataricus with , and as ligands. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus., Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A, Biochemistry. 2003 Dec 16;42(49):14397-407. PMID:14661950
Page seeded by OCA on Thu Feb 21 14:46:31 2008
Categories: Alcohol dehydrogenase | Single protein | Sulfolobus solfataricus | Bruno, I. | Esposito, L. | Giordano, A. | Mazzarella, L. | Raia, C A. | Rossi, M. | Sica, F. | Zagari, A. | ETX | NAD | ZN | Archaeon | Holoform | Nad(h) dependent | Zinc
