9.B.1.1.4 Ste24 endopeptidase, CAAX PP of 407 aas and 7 TMSs. The crystal structure has been solved showing that the Ste24p core structure is a ring of seven TMSs enclosing
a voluminous cavity containing the active site and substrate-binding
groove. The cavity is large enough to hold hundreds of water molecules, and is accessible to the external milieu by means of gaps
between splayed transmembrane helices (Sanders and Hutchison 2018). Possibly cleavage
proceeds by means of a processive mechanism of substrate insertion,
translocation, and ejection (Pryor et al. 2013). The active site is just under the interfacial lid of the barrel, with substrate entry and product exit through fenestrations located near the upper end of the barrel, just under the water-bilayer interface (Sanders and Hutchison 2018).
|
Accession Number: | J0MMU8 |
Protein Name: | Ste24 endopeptidase |
Length: | 407 |
Molecular Weight: | 46329.00 |
Species: | Helicobacter pylori Hp A-16 [992055] |
Number of TMSs: | 7 |
Substrate |
peptide, protein |
---|
1: MLDIWIDMII CIFYLLFFTT PYIVGDILQL KFIRQKLCEK PVLLPQKDYE EAGHYAIRKM
61: QLSIISQILD GIIFAGWVFF GLTHLEDLTH YLNLPETLGY LVFALLFLAI QSVLALPISY
121: YTTMHLDKEF GFSKVSLSLF FKDFFKGLSL TLGVGLLLIY TLIMIIEHVE HWEISSFFVV
181: FVFMILANLF YPKIAQLFNQ FTPLNNRDLE SQIESMMDKV GFKSEGIFVM DASKRDGRLN
241: AYFGGLGKNK RVVLFDTLIS KVGTEGLLAI LGHELGHFKN KDLLKSLGIM GGLLALVFAL
301: IAHLPPLVFE GFNVSQTPAS LIAILLLFLP VFSFYAMPLI GFFSRKNEYN ADKFGASLSS
361: KETLAKALVS IVNENKAFPY SHPFYVFLHF THPPLLERLK ALDYEIE