1nto

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|PDB= 1nto |SIZE=350|CAPTION= <scene name='initialview01'>1nto</scene>, resolution 1.94&Aring;
|PDB= 1nto |SIZE=350|CAPTION= <scene name='initialview01'>1nto</scene>, resolution 1.94&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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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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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE= ADH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 Sulfolobus solfataricus])
|GENE= ADH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 Sulfolobus solfataricus])
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|DOMAIN=
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|RELATEDENTRY=[[1jvb|1JVB]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nto OCA], [http://www.ebi.ac.uk/pdbsum/1nto PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nto RCSB]</span>
}}
}}
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[[Category: Sica, F.]]
[[Category: Sica, F.]]
[[Category: Zagari, A.]]
[[Category: Zagari, A.]]
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[[Category: ZN]]
 
[[Category: archaeon]]
[[Category: archaeon]]
[[Category: mutant]]
[[Category: mutant]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:35:23 2008''

Revision as of 19:35, 30 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
Related: 1JVB


Resources: FirstGlance, OCA, PDBsum, RCSB
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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