Structural highlights
Function
YQGQ_BACSU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the hypothetical protein YqgQ from Bacillus subtilis has been determined to 2.1 A resolution. The crystals belonged to space group P2(1), with unit-cell parameters a = 51.85, b = 41.25, c = 55.18 A, beta = 113.4 degrees , and contained three protein molecules in the asymmetric unit. The structure was determined by the single-wavelength anomalous dispersion method using selenium-labeled protein and was refined to a final R factor of 24.7% (R(free) = 28.0%). The protein molecule mainly comprises a three-helical bundle. Its putative function is inferred to be single-stranded nucleic acid binding based on sequence and structural homology.
Structure of YqgQ protein from Bacillus subtilis, a conserved hypothetical protein.,Lakshminarasimhan D, Eswaramoorthy S, Burley SK, Swaminathan S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt, 1):8-11. Epub 2009 Dec 25. PMID:20057058[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lakshminarasimhan D, Eswaramoorthy S, Burley SK, Swaminathan S. Structure of YqgQ protein from Bacillus subtilis, a conserved hypothetical protein. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt, 1):8-11. Epub 2009 Dec 25. PMID:20057058 doi:http://dx.doi.org/10.1107/S1744309109047009