1nto
From Proteopedia
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| - | [[Image:1nto.gif|left|200px]]<br /> | + | [[Image:1nto.gif|left|200px]]<br /><applet load="1nto" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1nto" size=" | + | |
caption="1nto, resolution 1.94Å" /> | caption="1nto, resolution 1.94Å" /> | ||
'''N249Y MUTANT OF ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS-MONOCLINIC CRYSTAL FORM'''<br /> | '''N249Y MUTANT OF ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS-MONOCLINIC CRYSTAL FORM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Alcohol dehydrogenase from Sulfolobus solfataricus (SsADH) is the only | + | Alcohol dehydrogenase from Sulfolobus solfataricus (SsADH) is the only enzyme from Archaea among the structurally studied members of the medium-chain ADH family described so far. Here, we present the three-dimensional structure of the apo form of the mutant N249Y which exhibits increased catalytic activity when compared to the wild-type enzyme. The substitution, located in the coenzyme binding domain, decreases the affinity for NAD(H) cofactor. The rearrangement of segments 248-250 and 270-275, induced by the mutation, suggests an explanation for the lower coenzyme affinity. This study also highlights the role in SsADH catalysis of the flexible loops located at the interface between the catalytic and the coenzyme domains. |
==About this Structure== | ==About this Structure== | ||
| - | 1NTO 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1NTO 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> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1NTO 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 14:09:57 2008'' |
Revision as of 12:09, 21 February 2008
|
N249Y MUTANT OF ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS-MONOCLINIC CRYSTAL FORM
Overview
Alcohol dehydrogenase from Sulfolobus solfataricus (SsADH) is the only enzyme from Archaea among the structurally studied members of the medium-chain ADH family described so far. Here, we present the three-dimensional structure of the apo form of the mutant N249Y which exhibits increased catalytic activity when compared to the wild-type enzyme. The substitution, located in the coenzyme binding domain, decreases the affinity for NAD(H) cofactor. The rearrangement of segments 248-250 and 270-275, induced by the mutation, suggests an explanation for the lower coenzyme affinity. This study also highlights the role in SsADH catalysis of the flexible loops located at the interface between the catalytic and the coenzyme domains.
About this Structure
1NTO is a Single protein structure of sequence from Sulfolobus solfataricus with as ligand. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Full crystallographic information is available from OCA.
Reference
Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity., Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A, FEBS Lett. 2003 Mar 27;539(1-3):14-8. PMID:12650918
Page seeded by OCA on Thu Feb 21 14:09:57 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. | ZN | Archaeon | Mutant | Nad(h)-dependent | Zinc
