Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Synechococcus phage S-SSM7 |
DNA and amino acid sequence determination and analysis, recombinant expression | Arabidopsis thaliana |
Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme, X-ray diffraction structure determination and analysis at 1.95 A resolution | Arabidopsis thaliana |
purified recombinant enzyme, X-ray diffraction structure determination and analysis at 1.95 A resolution, comparison to the crystal structure of the Arabidopsis thaliana chloroplast PDF enzyme | Synechococcus phage S-SSM7 |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | - |
Arabidopsis thaliana | 9507 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | catalytic zinc | Synechococcus phage S-SSM7 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | - |
- |
- |
Synechococcus phage S-SSM7 | E3SLL2 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity cromatography | Synechococcus phage S-SSM7 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme deformylates the N-terminal tetrapeptides from D1 proteins more efficiently than those from ribosomal proteins | Synechococcus phage S-SSM7 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
- |
Arabidopsis thaliana | |
- |
Synechococcus phage S-SSM7 |
General Information | Comment | Organism |
---|---|---|
evolution | phylogenetic analysis, the cyanophage enzyme belongs to the type 1B subclass, but lacking the C-terminal a-helix characteristic of that group. PDFs are a subclass of the metalloprotease superfamily of enzymes known as the clan MA and MB metalloproteases. Proteins from this family share a common structure containing a three-stranded beta strand facing a catalytic metal and a HEXXH motif-containing alpha helix. Activity of phage and bacterial PDFs on N-terminal tetrapeptides derived from D1 proteins and cyanobacterial ribosomal proteins, overview | Synechococcus phage S-SSM7 |
evolution | the enzyme belongs to the type 1B subclass.PDFs are a subclass of the metalloprotease superfamily of enzymes known as the clan MA and MB metalloproteases. Proteins from this family share a common structure containing a three-stranded beta strand facing a catalytic metal and a HEXXH motif-containing alpha helix | Arabidopsis thaliana |
physiological function | synthesis of functional proteins in bacteria requires co-translational removal of the N-terminal formyl group by a peptide deformylase, enzyme PDF expression during infection might benefit phage replication | Synechococcus phage S-SSM7 |