1seh

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[[Image:1seh.gif|left|200px]]
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{{STRUCTURE_1seh| PDB=1seh | SCENE= }}
{{STRUCTURE_1seh| PDB=1seh | SCENE= }}
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'''Crystal structure of E. coli dUTPase complexed with the product dUMP'''
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===Crystal structure of E. coli dUTPase complexed with the product dUMP===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15208312}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15208312 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15208312}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase., Barabas O, Pongracz V, Kovari J, Wilmanns M, Vertessy BG, J Biol Chem. 2004 Oct 8;279(41):42907-15. Epub 2004 Jun 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15208312 15208312]
Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase., Barabas O, Pongracz V, Kovari J, Wilmanns M, Vertessy BG, J Biol Chem. 2004 Oct 8;279(41):42907-15. Epub 2004 Jun 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15208312 15208312]
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Atomic resolution structure of Escherichia coli dUTPase determined ab initio., Gonzalez A, Larsson G, Persson R, Cedergren-Zeppezauer E, Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):767-74. Epub 2001, May 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11375495 11375495]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Enzyme-ligand complex]]
[[Category: Enzyme-ligand complex]]
[[Category: Jelly roll]]
[[Category: Jelly roll]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:36:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:36:14 2008''

Revision as of 18:36, 27 July 2008

Image:1seh.png

Template:STRUCTURE 1seh

Crystal structure of E. coli dUTPase complexed with the product dUMP

Template:ABSTRACT PUBMED 15208312

About this Structure

1SEH is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase., Barabas O, Pongracz V, Kovari J, Wilmanns M, Vertessy BG, J Biol Chem. 2004 Oct 8;279(41):42907-15. Epub 2004 Jun 17. PMID:15208312

Atomic resolution structure of Escherichia coli dUTPase determined ab initio., Gonzalez A, Larsson G, Persson R, Cedergren-Zeppezauer E, Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):767-74. Epub 2001, May 25. PMID:11375495

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