Stirrup protein domain
| Stirrup | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of an archaeal intein-encoded homing endonuclease pi-pfui | |||||||||
| Identifiers | |||||||||
| Symbol | Stirrup | ||||||||
| Pfam | PF09061 | ||||||||
| InterPro | IPR015146 | ||||||||
| SCOP2 | 1dq3 / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, the Stirrup is a protein domain found only in the domain archaea, in prokaryotic protein ribonucleotide reductases. It obtains its name due to its resemblance to an old fashioned Japanese stirrup. Stirrip has a molecular mass of 9 kDa and is folded into an alpha/beta structure. It allows for binding of the reductase to DNA via electrostatic interactions, since it has a predominance of positive charges distributed on its surface.[1]
Function
[edit]This protein domain provides the precursors necessary for DNA synthesis. It catalyses the biosynthesis of DNA from RNA.[2]
Structure
[edit]This structure contains a three-stranded beta-sheet to the solvent, which lies against alpha-helices.[1]
References
[edit]- ^ a b Ichiyanagi K, Ishino Y, Ariyoshi M, Komori K, Morikawa K (July 2000). "Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI". Journal of Molecular Biology. 300 (4): 889–901. doi:10.1006/jmbi.2000.3873. PMID 10891276.
- ^ "Ribonucleoside-diphosphate reductase". UniProt. Retrieved 14 August 2012.