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 protein domain Stirrup is a domain, found only in found in the domain, archaea. The Stirrup protein domain is found in prokaryotic protein ribonucleotide reductases. It obtains its name due to its resemblance to a 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
This protein domain provides the precursors necessary for DNA synthesis. It catalyses the biosynthesis of deoxyribonucleotides from ribonucleotides[1].
Structure
This structure contains a three-stranded beta-sheet to the solvent, which lies against alpha-helices[1].
References
- ^ a b Ichiyanagi K, Ishino Y, Ariyoshi M, Komori K, Morikawa K (2000). "Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI". J. Mol. Biol. 300 (4): 889–901. doi:10.1006/jmbi.2000.3873. PMID 10891276.
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