2hrm: Difference between revisions

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==Overview==

dUTPase is essential to keep uracil out of DNA. Crystal structures of, substrate (dUTP and alpha,beta-imino-dUTP) and product complexes of wild, type and mutant dUTPases were determined to reveal how an enzyme, responsible for DNA integrity functions. A kinetic analysis of wild type, and mutant dUTPases was performed to obtain relevant mechanistic, information in solution. Substrate hydrolysis is shown to be initiated via, in-line nucleophile attack of a water molecule oriented by an activating, conserved aspartate residue. Substrate binding in a catalytically, competent conformation is achieved by (i) multiple interactions of the, triphosphate moiety with catalysis-assisting Mg2+, (ii) a concerted motion, of residues from three conserved enzyme motifs as compared with the, apoenzyme, and (iii) an intricate hydrogen-bonding network that includes, several water molecules in the active site. Results provide an, understanding for the catalytic role of conserved residues in dUTPases.

dUTPase is essential to keep uracil out of DNA. Crystal structures of substrate (dUTP and alpha,beta-imino-dUTP) and product complexes of wild type and mutant dUTPases were determined to reveal how an enzyme responsible for DNA integrity functions. A kinetic analysis of wild type and mutant dUTPases was performed to obtain relevant mechanistic information in solution. Substrate hydrolysis is shown to be initiated via in-line nucleophile attack of a water molecule oriented by an activating conserved aspartate residue. Substrate binding in a catalytically competent conformation is achieved by (i) multiple interactions of the triphosphate moiety with catalysis-assisting Mg2+, (ii) a concerted motion of residues from three conserved enzyme motifs as compared with the apoenzyme, and (iii) an intricate hydrogen-bonding network that includes several water molecules in the active site. Results provide an understanding for the catalytic role of conserved residues in dUTPases.

==About this Structure==

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[[Category: Kovari, J.]]

[[Category: Tapai, R]]

[[Category: Vertessy, B.G.]]

[[Category: Vertessy, B G.]]

[[Category: EDO]]

[[Category: UC5]]

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[[Category: jelly roll]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:59 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-dUTPase is essential to keep uracil out of DNA. Crystal structures of, substrate (dUTP and alpha,beta-imino-dUTP) and product complexes of wild, type and mutant dUTPases were determined to reveal how an enzyme, responsible for DNA integrity functions. A kinetic analysis of wild type, and mutant dUTPases was performed to obtain relevant mechanistic, information in solution. Substrate hydrolysis is shown to be initiated via, in-line nucleophile attack of a water molecule oriented by an activating, conserved aspartate residue. Substrate binding in a catalytically, competent conformation is achieved by (i) multiple interactions of the, triphosphate moiety with catalysis-assisting Mg2+, (ii) a concerted motion, of residues from three conserved enzyme motifs as compared with the, apoenzyme, and (iii) an intricate hydrogen-bonding network that includes, several water molecules in the active site. Results provide an, understanding for the catalytic role of conserved residues in dUTPases.
+dUTPase is essential to keep uracil out of DNA. Crystal structures of substrate (dUTP and alpha,beta-imino-dUTP) and product complexes of wild type and mutant dUTPases were determined to reveal how an enzyme responsible for DNA integrity functions. A kinetic analysis of wild type and mutant dUTPases was performed to obtain relevant mechanistic information in solution. Substrate hydrolysis is shown to be initiated via in-line nucleophile attack of a water molecule oriented by an activating conserved aspartate residue. Substrate binding in a catalytically competent conformation is achieved by (i) multiple interactions of the triphosphate moiety with catalysis-assisting Mg2+, (ii) a concerted motion of residues from three conserved enzyme motifs as compared with the apoenzyme, and (iii) an intricate hydrogen-bonding network that includes several water molecules in the active site. Results provide an understanding for the catalytic role of conserved residues in dUTPases.
 ==About this Structure==
@@ Line 17: / Line 17: @@
 [[Category: Kovari, J.]]
 [[Category: Tapai, R]]
-[[Category: Vertessy, B.G.]]
+[[Category: Vertessy, B G.]]
 [[Category: EDO]]
 [[Category: UC5]]
@@ Line 24: / Line 24: @@
 [[Category: jelly roll]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:20:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:59 2008''