1dud
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=DUD:DEOXYURIDINE-5'-DIPHOSPHATE'>DUD</scene> | |LIGAND= <scene name='pdbligand=DUD:DEOXYURIDINE-5'-DIPHOSPHATE'>DUD</scene> | ||
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dud OCA], [http://www.ebi.ac.uk/pdbsum/1dud PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dud RCSB]</span> | ||
}} | }} | ||
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[[Category: Nyman, P O.]] | [[Category: Nyman, P O.]] | ||
[[Category: Svensson, L A.]] | [[Category: Svensson, L A.]] | ||
| - | [[Category: DUD]] | ||
[[Category: d-udp complex]] | [[Category: d-udp complex]] | ||
[[Category: d-utpase]] | [[Category: d-utpase]] | ||
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[[Category: substrate analogue]] | [[Category: substrate analogue]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:48:50 2008'' |
Revision as of 16:48, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | dUTP diphosphatase, with EC number 3.6.1.23 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDE HYDROLASE (D-UTPASE) COMPLEXED WITH THE SUBSTRATE ANALOGUE DEOXYURIDINE 5'-DIPHOSPHATE (D-UDP)
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.
About this Structure
1DUD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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