Title : Structural basis for type VI secreted peptidoglycan DL-endopeptidase function, specificity and neutralization in Serratia marcescens.

Pub. Date : 2013 Dec

PMID : 24311588






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 These small secreted proteins, Ssp1 and Ssp2, cleave between gamma-D-glutamic acid and L-meso-diaminopimelic acid with different specificities. D-glutamic acid SUMO specific peptidase 6 Homo sapiens
2 These small secreted proteins, Ssp1 and Ssp2, cleave between gamma-D-glutamic acid and L-meso-diaminopimelic acid with different specificities. l-meso-diaminopimelic acid SUMO specific peptidase 6 Homo sapiens
3 Ssp1 displays greater promiscuity and cleaves monomeric tripeptides, tetrapeptides and pentapeptides and dimeric tetratetra and tetrapenta muropeptides on both the acceptor and donor strands. tripeptides SUMO specific peptidase 6 Homo sapiens
4 Ssp1 displays greater promiscuity and cleaves monomeric tripeptides, tetrapeptides and pentapeptides and dimeric tetratetra and tetrapenta muropeptides on both the acceptor and donor strands. tetratetra SUMO specific peptidase 6 Homo sapiens
5 Ssp1 displays greater promiscuity and cleaves monomeric tripeptides, tetrapeptides and pentapeptides and dimeric tetratetra and tetrapenta muropeptides on both the acceptor and donor strands. tetrapenta muropeptides SUMO specific peptidase 6 Homo sapiens
6 Functional assays confirm the identity of a catalytic cysteine in these endopeptidases and crystal structures provide information on the structure-activity relationships of Ssp1 and, by comparison, of related effectors. Cysteine SUMO specific peptidase 6 Homo sapiens