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1lau
From Proteopedia
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|PDB= 1lau |SIZE=350|CAPTION= <scene name='initialview01'>1lau</scene>, resolution 1.800Å | |PDB= 1lau |SIZE=350|CAPTION= <scene name='initialview01'>1lau</scene>, resolution 1.800Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lau OCA], [http://www.ebi.ac.uk/pdbsum/1lau PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lau RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LAU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1LAU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAU OCA]. |
==Reference== | ==Reference== | ||
The structural basis of specific base-excision repair by uracil-DNA glycosylase., Savva R, McAuley-Hecht K, Brown T, Pearl L, Nature. 1995 Feb 9;373(6514):487-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7845459 7845459] | The structural basis of specific base-excision repair by uracil-DNA glycosylase., Savva R, McAuley-Hecht K, Brown T, Pearl L, Nature. 1995 Feb 9;373(6514):487-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7845459 7845459] | ||
| - | [[Category: Human herpesvirus | + | [[Category: Human herpesvirus 1]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Pearl, L H.]] | [[Category: Pearl, L H.]] | ||
| Line 28: | Line 31: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:00:29 2008'' |
Revision as of 19:00, 30 March 2008
| |||||||
| , resolution 1.800Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
URACIL-DNA GLYCOSYLASE
Overview
The 1.75-A crystal structure of the uracil-DNA glycosylase from herpes simplex virus type-1 reveals a new fold, distantly related to dinucleotide-binding proteins. Complexes with a trideoxynucleotide, and with uracil, define the DNA-binding site and allow a detailed understanding of the exquisitely specific recognition of uracil in DNA. The overall structure suggests binding models for elongated single- and double-stranded DNA substrates. Conserved residues close to the uracil-binding site suggest a catalytic mechanism for hydrolytic base excision.
About this Structure
1LAU is a Single protein structure of sequence from Human herpesvirus 1. Full crystallographic information is available from OCA.
Reference
The structural basis of specific base-excision repair by uracil-DNA glycosylase., Savva R, McAuley-Hecht K, Brown T, Pearl L, Nature. 1995 Feb 9;373(6514):487-93. PMID:7845459
Page seeded by OCA on Sun Mar 30 22:00:29 2008
