This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1lau
From Proteopedia
(New page: 200px<br /><applet load="1lau" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lau, resolution 1.800Å" /> '''URACIL-DNA GLYCOSYL...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1lau.jpg|left|200px]]<br /><applet load="1lau" size=" | + | [[Image:1lau.jpg|left|200px]]<br /><applet load="1lau" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lau, resolution 1.800Å" /> | caption="1lau, resolution 1.800Å" /> | ||
'''URACIL-DNA GLYCOSYLASE'''<br /> | '''URACIL-DNA GLYCOSYLASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 1.75-A crystal structure of the uracil-DNA glycosylase from herpes | + | 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== | ==About this Structure== | ||
| - | 1LAU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http:// | + | 1LAU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAU OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Pearl, L | + | [[Category: Pearl, L H.]] |
[[Category: Savva, R.]] | [[Category: Savva, R.]] | ||
[[Category: dna]] | [[Category: dna]] | ||
| Line 19: | Line 19: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:12 2008'' |
Revision as of 11:43, 21 February 2008
|
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 4. 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 Thu Feb 21 13:43:12 2008
