Characterization of a polypeptide‐binding site in the  DEAD  Motor of the SecA  ATP ase | Zendy

Khalili Yazdi Aliakbar | Zendy; Namjoshi Sarita | Zendy; Hackett Jesse | Zendy; Ghonaim Nour | Zendy; Shilton Brian H. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

Characterization of a polypeptide‐binding site in the DEAD Motor of the SecA ATP ase

Author(s) -

Khalili Yazdi Aliakbar,

Namjoshi Sarita,

Hackett Jesse,

Ghonaim Nour,

Shilton Brian H.

Publication year - 2017

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1002/1873-3468.12832

Subject(s) - maltose binding protein , surface plasmon resonance , peptide , chemistry , cyclic nucleotide binding domain , binding site , atpase , biochemistry , plasma protein binding , binding protein , binding domain , peptide sequence , biophysics , biology , enzyme , fusion protein , recombinant dna , gene , nanotechnology , materials science , nanoparticle

We coupled peptides from a CNB r digest of signal‐sequenceless maltose‐binding protein ( MBP ) to a surface plasmon resonance chip. SecA‐N95, SecA‐N68, and SecA‐ DM (which consists of only the DEAD Motor domains NBD 1 and NBD 2) bound to the immobilized peptides; ADP weakened the binding. SecA‐ DM , which lacks the ‘preprotein cross‐linking domain’ ( PPXD ), displayed the most extensive binding, while an MBP ‐ PPXD chimera showed no binding, demonstrating that the PPXD does not contribute to the binding. We characterized the sequence specificity using oriented peptide libraries; these results enabled synthesis of a 20‐residue peptide that was used to recapitulate the results obtained with MBP ‐derived peptides. This study shows that there is a promiscuous and nucleotide‐modulated peptide‐binding site in the DEAD Motor domains of SecA.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research