SURA E.Coli
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Description
SURA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 429 amino acids (21-428 a.a.) and having a molecular weight of 47.3kDa. The SURA is fused to 20 a.a His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MAPQVVDKVA AVVNNGVVLE SDVDGLMQSV KLNAAQARQQ LPDDATLRHQ IMERLIMDQI ILQMGQKMGV KISDEQLDQA IANIAKQNNM TLDQMRSRLA YDGLNYNTYR NQIRKEMIIS EVRNNEVRRR ITILPQEVES LAQQVGNQND ASTELNLSHI LIPLPENPTS DQVNEAESQA RAIVDQARNG ADFGKLAIAH SADQQALNGG QMGWGRIQEL PGIFAQALST AKKGDIVGPI RSGVGFHILK VNDLRGESKN ISVTEVHARH ILLKPSPIMT DEQARVKLEQ IAADIKSGKT TFAAAAKEFS QDPGSANQGG DLGWATPDIF DPAFRDALTR LNKGQMSAPV HSSFGWHLIE LLDTRNVDKT DAAQKDRAYR MLMNRKFSEE AASWMQEQRA SAYVKILSN.
Product Science Overview
Introduction
Chaperones are essential proteins that assist in the proper folding of other proteins, preventing misfolding and aggregation. In Escherichia coli (E. coli), several chaperones play crucial roles in maintaining protein homeostasis. One such chaperone is SurA, which is particularly important for the biogenesis of outer membrane proteins (OMPs).
SurA Chaperone
SurA (Survival protein A) is a periplasmic chaperone in E. coli that is involved in the folding and assembly of OMPs. It is part of a network of chaperones that includes Skp and DegP, which together ensure the proper folding and insertion of OMPs into the outer membrane. SurA has peptidyl-prolyl isomerase (PPIase) activity, which helps in the isomerization of peptide bonds at proline residues, a critical step in protein folding.
Role in Outer Membrane Protein Biogenesis
The biogenesis of OMPs is a complex process that begins in the cytoplasm, where the proteins are synthesized. They are then translocated across the inner membrane into the periplasm via the Sec or Tat pathways. In the periplasm, chaperones like SurA bind to the nascent OMPs, preventing their aggregation and guiding them to the Bam (β-barrel assembly machinery) complex in the outer membrane. The Bam complex then facilitates the insertion and folding of OMPs into the outer membrane.
Importance of SurA
SurA is considered the primary chaperone for OMPs in E. coli. Studies have shown that the deletion of the surA gene leads to severe defects in OMP assembly, resulting in compromised cell viability and increased sensitivity to environmental stresses. SurA’s role is particularly crucial under conditions where the demand for OMP assembly is high, such as during rapid cell growth or stress responses.
Recombinant Expression of SurA
The recombinant expression of SurA in E. coli has been explored to enhance the production of soluble and functional recombinant proteins. Overexpression of SurA can improve the folding efficiency of target proteins, reducing the formation of inclusion bodies and increasing the yield of soluble proteins. This approach is particularly useful in biotechnology and pharmaceutical industries, where high yields of correctly folded proteins are essential.
Conclusion
SurA is a vital chaperone in E. coli, playing a key role in the biogenesis of outer membrane proteins. Its ability to assist in protein folding and prevent aggregation makes it an important tool in recombinant protein production. Understanding the function and mechanism of SurA can lead to improved strategies for producing high-quality recombinant proteins in E. coli.
