Stirrup protein domain

Last updated
Stirrup
PDB 1dq3 EBI.jpg
crystal structure of an archaeal intein-encoded homing endonuclease pi-pfui
Identifiers
SymbolStirrup
Pfam PF09061
InterPro IPR015146
SCOP2 1dq3 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

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]

Contents

Function

This protein domain provides the precursors necessary for DNA synthesis. It catalyses the biosynthesis of DNA from RNA. [2]

Structure

This structure contains a three-stranded beta-sheet to the solvent, which lies against alpha-helices. [1]

References

  1. 1 2 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.
  2. "Ribonucleoside-diphosphate reductase". UniProt. Retrieved 14 August 2012.
This article incorporates text from the public domain Pfam and InterPro: IPR015146