2hrm
From Proteopedia
(New page: 200px<br /><applet load="2hrm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hrm, resolution 1.70Å" /> '''Crystal structure of...) |
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| - | [[Image:2hrm.jpg|left|200px]]<br /><applet load="2hrm" size=" | + | [[Image:2hrm.jpg|left|200px]]<br /><applet load="2hrm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2hrm, resolution 1.70Å" /> | caption="2hrm, resolution 1.70Å" /> | ||
'''Crystal structure of dUTPase complexed with substrate analogue methylene-dUTP'''<br /> | '''Crystal structure of dUTPase complexed with substrate analogue methylene-dUTP'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with UC5 and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.23 3.6.1.23] Full crystallographic information is available from [http:// | + | 2HRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=UC5:'>UC5</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.23 3.6.1.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HRM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: jelly roll]] | [[Category: jelly roll]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:20:37 2008'' |
Revision as of 12:20, 23 January 2008
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Crystal structure of dUTPase complexed with substrate analogue methylene-dUTP
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.
About this Structure
2HRM is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as dUTP diphosphatase, with EC number 3.6.1.23 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
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