1nto

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[[Image:1nto.gif|left|200px]]<br /><applet load="1nto" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nto.gif|left|200px]]
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caption="1nto, resolution 1.94&Aring;" />
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'''N249Y MUTANT OF ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS-MONOCLINIC CRYSTAL FORM'''<br />
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{{Structure
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|PDB= 1nto |SIZE=350|CAPTION= <scene name='initialview01'>1nto</scene>, resolution 1.94&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY= [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]
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|GENE= ADH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 Sulfolobus solfataricus])
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}}
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'''N249Y MUTANT OF ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS-MONOCLINIC CRYSTAL FORM'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1NTO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NTO OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12650918 12650918]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12650918 12650918]
[[Category: Alcohol dehydrogenase]]
[[Category: Alcohol dehydrogenase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:33 2008''

Revision as of 11:01, 20 March 2008


PDB ID 1nto

Drag the structure with the mouse to rotate
, resolution 1.94Å
Ligands:
Gene: ADH (Sulfolobus solfataricus)
Activity: Alcohol dehydrogenase, with EC number 1.1.1.1
Coordinates: save as pdb, mmCIF, xml



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. 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

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