1dud: Difference between revisions

Revision as of 13:20, 21 February 2008

DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDE HYDROLASE (D-UTPASE) COMPLEXED WITH THE SUBSTRATE ANALOGUE DEOXYURIDINE 5'-DIPHOSPHATE (D-UDP)

OverviewOverview

We have determined the structure of the homotrimeric dUTPase from Escherichia coli, completed with an inhibitor and substrate analogue, dUDP. Three molecules of dUDP are found symmetrically bound per trimer, each in a shallow cleft between adjacent subunits, interacting with evolutionary conserved residues. The interactions of the uracil ring and the deoxypentose with the protein are consistent with the high specificity of the enzyme with respect to these groups. The positions of the two phosphate groups and adjacent water molecules are discussed in relation to the mechanism and kinetics of catalysis. The role that dUTPase plays in DNA metabolism makes the enzyme a potential target for chemotherapeutic drugs: the results presented here will aid in the design and development of inhibitory compounds.

About this StructureAbout this Structure

1DUD is a Single protein structure of sequence from Escherichia coli with as ligand. Active as dUTP diphosphatase, with EC number 3.6.1.23 Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP)., Larsson G, Svensson LA, Nyman PO, Nat Struct Biol. 1996 Jun;3(6):532-8. PMID:8646539

Page seeded by OCA on Thu Feb 21 12:20:33 2008

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OCA

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-[[Image:1dud.gif|left|200px]]<br /><applet load="1dud" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dud.gif|left|200px]]<br /><applet load="1dud" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dud, resolution 2.3&Aring;" />
 '''DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDE HYDROLASE (D-UTPASE) COMPLEXED WITH THE SUBSTRATE ANALOGUE DEOXYURIDINE 5'-DIPHOSPHATE (D-UDP)'''<br />
 ==Overview==
-We have determined the structure of the homotrimeric dUTPase from, Escherichia coli, completed with an inhibitor and substrate analogue, dUDP. Three molecules of dUDP are found symmetrically bound per trimer, each in a shallow cleft between adjacent subunits, interacting with, evolutionary conserved residues. The interactions of the uracil ring and, the deoxypentose with the protein are consistent with the high specificity, of the enzyme with respect to these groups. The positions of the two, phosphate groups and adjacent water molecules are discussed in relation to, the mechanism and kinetics of catalysis. The role that dUTPase plays in, DNA metabolism makes the enzyme a potential target for chemotherapeutic, drugs: the results presented here will aid in the design and development, of inhibitory compounds.
+We have determined the structure of the homotrimeric dUTPase from Escherichia coli, completed with an inhibitor and substrate analogue, dUDP. Three molecules of dUDP are found symmetrically bound per trimer, each in a shallow cleft between adjacent subunits, interacting with evolutionary conserved residues. The interactions of the uracil ring and the deoxypentose with the protein are consistent with the high specificity of the enzyme with respect to these groups. The positions of the two phosphate groups and adjacent water molecules are discussed in relation to the mechanism and kinetics of catalysis. The role that dUTPase plays in DNA metabolism makes the enzyme a potential target for chemotherapeutic drugs: the results presented here will aid in the design and development of inhibitory compounds.
 ==About this Structure==
-DUD 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 DUD as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DUD OCA].
+DUD 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=DUD:'>DUD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1DUD OCA].
 ==Reference==
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 [[Category: dUTP diphosphatase]]
 [[Category: Larsson, G.]]
-[[Category: Nyman, P.O.]]
+[[Category: Nyman, P O.]]
-[[Category: Svensson, L.A.]]
+[[Category: Svensson, L A.]]
 [[Category: DUD]]
 [[Category: d-udp complex]]
@@ Line 24: / Line 24: @@
 [[Category: substrate analogue]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:35:35 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:33 2008''