Purification, characterization, and crystallization of the adhesive domain of SdrD from Staphylococcus aureus

Zhang, Liqing; Xiang, Hua; Gao, Jinlan; Hu, Jia; Miao, Shiying; Wang, Linfang; Deng, Xuming; Li, Shentao

doi:10.1016/j.pep.2009.09.007

Cited by 8 publications

(5 citation statements)

References 17 publications

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“…The selenomethionine (Se-Met) protein of SdrD 235-551 was expressed and purifi ed similarly. Protein in each step was analyzed by SDS-PAGE Coomassie Brilliant Blue staining (Zhang et al, 2010). issue, and far from fully understood. Instead of attempting various traditional antibiotics, blocking or modifying S. aureus adhering ability could interfere with its survival and invasion.…”

Section: Protein Cellmentioning

confidence: 99%

Structures of SdrD from Staphylococcus aureus reveal the molecular mechanism of how the cell surface receptors recognize their ligands

Wang

Liu

et al. 2013

Protein Cell

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Section: Protein Cellmentioning

confidence: 99%

Structures of SdrD from Staphylococcus aureus reveal the molecular mechanism of how the cell surface receptors recognize their ligands

Wang

Liu

et al. 2013

Protein Cell

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“…Sample preparation for mass-spectrometric analysis was performed as described previously (Zhang et al, 2010). MALDI-TOF-TOF analysis was performed on an ultra-fleXtreme mass spectrometer (Bruker Daltonics, Bremen, Germany).…”

Section: Maldi-tof-tof Mass-spectrometric Analysismentioning

confidence: 99%

Structure of the branched-chain aminotransferase fromStreptococcus mutans

Ruan

Yin

et al. 2012

Acta Crystallogr D Biol Cryst

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The branched‐chain amino‐acid aminotransferase from Streptococcus mutans (SmIlvE) was recombinantly expressed in Escherichia coli with high yield. An effective purification protocol was established. A bioactivity assay indicated that SmIlvE had aminotransferase activity. The specific activity of SmIlvE towards amino‐acid substrates was found to be as follows (in descending order): Ile > Leu > Val > Trp > Gly. The protein was crystallized using the hanging‐drop vapour‐diffusion method with PEG 3350 as the primary precipitant. The structure of SmIlvE was solved at 1.97 Å resolution by the molecular‐replacement method. Comparison with structures of homologous proteins enabled the identification of conserved structural elements that might play a role in substrate binding. Further work is needed to confirm the interaction between SmIlvE and its substrates by determining the structures of their complexes.

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“…The purified protein was analyzed by SDS-PAGE and MALDI-TOF MS as reported elsewhere (Zhang et al, 2010). Total proteins were measured using the Bradford method (Bradford, 1976).…”

Section: Cloning Expression and Purificationmentioning

confidence: 99%

Crystallization and preliminary X-ray analysis ofS-ribosylhomocysteinase fromStreptococcus mutans

Zhao

Zhu

et al. 2012

Acta Cryst Sect F

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S-Ribosylhomocysteinase (LuxS) encoded by theluxSgene fromStreptococcus mutansplays a crucial role in the quorum-sensing system. LuxS was solubly expressed inEscherichia coliwith high yield. The purity of the purified target protein, which was identified by SDS–PAGE and MALDI–TOF MS analysis, was >95%. The protein was crystallized using the hanging-drop vapour-diffusion method with PEG 3350 as the primary precipitant. X-ray diffraction data were collected at Beijing Synchrotron Radiation Facility (BSRF). Diffraction by the crystal extended to 2.4 Å resolution and the crystal belonged to space groupC2221, with unit-cell parametersa= 55.3,b= 148.7,c= 82.8 Å.

show abstract

Purification, characterization, and crystallization of the adhesive domain of SdrD from Staphylococcus aureus

Cited by 8 publications

References 17 publications

Structures of SdrD from Staphylococcus aureus reveal the molecular mechanism of how the cell surface receptors recognize their ligands

Structures of SdrD from Staphylococcus aureus reveal the molecular mechanism of how the cell surface receptors recognize their ligands

Structure of the branched-chain aminotransferase fromStreptococcus mutans

Crystallization and preliminary X-ray analysis ofS-ribosylhomocysteinase fromStreptococcus mutans

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