Structure of YqgQ protein from Bacillus subtilis, a conserved hypothetical protein

Damodharan Lakshminarasimhan; Subramaniam Eswaramoorthy; Stephen K. Burley; Subramanyam Swaminathan

doi:10.1107/S1744309109047009

Structure of YqgQ protein from Bacillus subtilis, a conserved hypothetical protein

Damodharan Lakshminarasimhan, Subramaniam Eswaramoorthy, Stephen K. Burley, Subramanyam Swaminathan

Research output: Contribution to journal › Article › peer-review

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Abstract

The crystal structure of the hypothetical protein YqgQ from Bacillus subtilis has been determined to 2.1 Å resolution. The crystals belonged to space group P21, with unit-cell parameters a = 51.85, b = 41.25, c = 55.18 Å, Β = 113.4°, 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.

Original language	English (US)
Pages (from-to)	8-11
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	66
Issue number	1
DOIs	https://doi.org/10.1107/S1744309109047009
State	Published - Dec 25 2009
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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abstract = "The crystal structure of the hypothetical protein YqgQ from Bacillus subtilis has been determined to 2.1 {\AA} resolution. The crystals belonged to space group P21, with unit-cell parameters a = 51.85, b = 41.25, c = 55.18 {\AA}, Β = 113.4°, 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% (Rfree = 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.",

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AU - Lakshminarasimhan, Damodharan

AU - Eswaramoorthy, Subramaniam

AU - Burley, Stephen K.

AU - Swaminathan, Subramanyam

PY - 2009/12/25

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AB - The crystal structure of the hypothetical protein YqgQ from Bacillus subtilis has been determined to 2.1 Å resolution. The crystals belonged to space group P21, with unit-cell parameters a = 51.85, b = 41.25, c = 55.18 Å, Β = 113.4°, 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% (Rfree = 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.

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Structure of YqgQ protein from Bacillus subtilis, a conserved hypothetical protein

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