1nvg: Difference between revisions

Revision as of 15:10, 21 February 2008

N249Y MUTANT OF THE ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS-TETRAGONAL CRYSTAL FORM

OverviewOverview

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 StructureAbout this Structure

1NVG is a Single protein structure of sequence from Sulfolobus solfataricus with as ligand. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

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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 ==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.
+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==
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 [[Category: Giordano, A.]]
 [[Category: Mazzarella, L.]]
-[[Category: Raia, C.A.]]
+[[Category: Raia, C A.]]
 [[Category: Rossi, M.]]
 [[Category: Sica, F.]]
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 [[Category: zinc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:54:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:30 2008''