1scj: Difference between revisions

We report here the crystallographic structure determination of an, autoprocessed (Ser221Cys)-subtilisin E-propeptide complex at 2.0 A, resolution. The subtilisin domain sequence has a single substitution, (Ser221Cys) which has been shown to block the maturation process prior to, degradation of the propeptide domain (77 residues) that acts as an, intramolecular chaperon. This mutation, however, did not prevent the, enzyme from cleaving its propeptide domain with a 60-80% efficiency. The, current determination is the first example of a subtilisin E-propeptide, complex which has been autoprocessed. A previous structure determination, of a BPN'-prosegment complex has been reported in which the subtilisin, domain was extensively mutated and a calcium binding loop was deleted., Further, in this earlier determination, the complex was formed by the, addition of separately expressed propeptide domain. The structure, determination reported here provides additional information about the, nature of the interaction between the subtilisin and propeptide domains in, this complex.

1SCJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Structure known Active Site: AVE. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SCJ OCA].  

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