Refine
Has Fulltext
- yes (15)
Is part of the Bibliography
- yes (15)
Document Type
- Journal article (15)
Language
- English (15)
Keywords
- phosphorylation (3)
- actin (2)
- protein (2)
- ADP-ribosyltransferases (1)
- Arp2/3 complex (1)
- BRAF (1)
- Clostridioides binary toxins (1)
- ESAT‐6‐like secretion system (1)
- ESS (1)
- Entwicklung (1)
- EsaA (1)
- FoxO3 (1)
- H2A histone family member X (H2AX) (1)
- Lebenszyklus (1)
- M14 carboxypeptidasses (1)
- MAX (1)
- MYCN (1)
- Profilierung (1)
- RHO (1)
- RHO-associated kinease (1)
- RNA splicing (1)
- ROK-alpha (1)
- Ribosom (1)
- Staphylococcus aureus USA300 (1)
- TRRAP (1)
- Trypanosoma brucei (1)
- Wilms tumor (1)
- activating transcription factor 4 (ATF4) (1)
- activation (1)
- ancistrocladinium A (1)
- ataxia teleagiectasia mutated (ATM) (1)
- bacterial transcription (1)
- cancer therapy (1)
- cell wall synthesis (1)
- cells (1)
- cellular stress response (1)
- convergent extension movements (1)
- direct muss spectrometric profiling (1)
- domain (1)
- extracellular domain (1)
- factor-I (1)
- friut fly behaviour (1)
- gene (1)
- interactome (1)
- laminin receptor (1)
- localization (1)
- membrane (1)
- morphogenesis (1)
- multiple myeloma (1)
- mutation screening (1)
- mutation triggers (1)
- naphthylisoquinoline alkaloids (1)
- pathogens (1)
- peptidomoics (1)
- planar cell polarity (1)
- proteasome inhibitor resistance (1)
- proteasome subunit beta type-5 (PSMB5) (1)
- protein processing (1)
- protein-protein interaction (1)
- proteomics (1)
- sorafenib (1)
- toxin (1)
- transcription factors (1)
- translocation (1)
- tumour-necrosis factors (1)
- type VII secretion system (1)
Institute
- Rudolf-Virchow-Zentrum (14)
- Comprehensive Cancer Center Mainfranken (4)
- Theodor-Boveri-Institut für Biowissenschaften (3)
- Institut für Molekulare Infektionsbiologie (2)
- Institut für Organische Chemie (1)
- Institut für Pharmakologie und Toxikologie (1)
- Klinik und Poliklinik für Dermatologie, Venerologie und Allergologie (1)
- Medizinische Fakultät (1)
- Medizinische Klinik und Poliklinik I (1)
- Medizinische Klinik und Poliklinik II (1)
Sonstige beteiligte Institutionen
EU-Project number / Contract (GA) number
The membrane protein EsaA is a conserved component of the type VIIb secretion system. Limited proteolysis of purified EsaA from Staphylococcus aureus USA300 identified a stable 48 kDa fragment, which was mapped by fingerprint mass spectrometry to an uncharacterized extracellular segment of EsaA. Analysis by circular dichroism spectroscopy showed that this fragment folds into a single stable domain made of mostly α‐helices with a melting point of 34.5°C. Size‐exclusion chromatography combined with multi‐angle light scattering indicated the formation of a dimer of the purified extracellular domain. Octahedral crystals were grown in 0.2 M ammonium citrate tribasic pH 7.0, 16% PEG 3350 using the hanging‐drop vapor‐diffusion method. Diffraction data were analyzed to 4.0 Å resolution, showing that the crystals belonged to the enantiomorphic tetragonal space groups P41212 or P43212, with unit‐cell parameters a = 197.5, b = 197.5, c = 368.3 Å, α = β = γ = 90°.