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.
1nom
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1nom.png|left|200px]] | ||
| - | |||
{{STRUCTURE_1nom| PDB=1nom | SCENE= }} | {{STRUCTURE_1nom| PDB=1nom | SCENE= }} | ||
| - | |||
===DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7), 31-KD DOMAIN; SOAKED IN THE PRESENCE OF MNCL2 (5 MILLIMOLAR)=== | ===DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7), 31-KD DOMAIN; SOAKED IN THE PRESENCE OF MNCL2 (5 MILLIMOLAR)=== | ||
| + | {{ABSTRACT_PUBMED_8841120}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/DPOLB_RAT DPOLB_RAT]] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. | ||
==About this Structure== | ==About this Structure== | ||
| Line 14: | Line 13: | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:008841120</ref><references group="xtra"/> | + | <ref group="xtra">PMID:008841120</ref><references group="xtra"/><references/> |
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
Revision as of 07:52, 27 March 2013
Contents |
DNA POLYMERASE BETA (POL B) (E.C.2.7.7.7), 31-KD DOMAIN; SOAKED IN THE PRESENCE OF MNCL2 (5 MILLIMOLAR)
Template:ABSTRACT PUBMED 8841120
Function
[DPOLB_RAT] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.
About this Structure
1nom is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
See Also
Reference
- Pelletier H, Sawaya MR. Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymerase beta by X-ray structural analysis. Biochemistry. 1996 Oct 1;35(39):12778-87. PMID:8841120 doi:http://dx.doi.org/10.1021/bi960790i
