Crystal and solution structures of a prokaryotic M16B peptidase: an open and shut case.
Crystal and solution structures of a prokaryotic M16B peptidase: an open and shut case.
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DOI:
10.1016/j.str.2009.09.009
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发表时间:
2009-11-11
期刊:
影响因子:
--
通讯作者:
Smith JW
中科院分区:
文献类型:
--
作者:
Aleshin AE;Gramatikova S;Hura GL;Bobkov A;Strongin AY;Stec B;Tainer JA;Liddington RC;Smith JW
The M16 family of zinc peptidases comprises a pair of homologous domains that form two halves of a ‘‘clam-shell’’ surrounding the active site. The M16A and M16C subfamilies form one class (‘‘peptidasomes’’): they degrade 30–70 residue peptides, and adopt both open and closed conformations. The eukaryotic M16B subfamily forms a second class (‘‘processing proteases’’): they adopt a single partly-open conformation that enables them to cleave signal sequences from larger proteins. Here, we report the solution and crystal structures of a prokaryotic M16B peptidase, and demonstrate that it has features of both classes: thus, it forms stable ‘‘open’’ homodimers in solution that resemble the processing proteases; but the clam-shell closes upon binding substrate, a feature of the M16A/C peptidasomes. Moreover, clam-shell closure is required for proteolytic activity. We predict that other prokaryotic M16B family members will form dimeric peptidasomes, and propose a model for the evolution of the M16 family.
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影响因子:
3.7
作者:
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通讯作者:
Leissring MA
DOI:
10.1107/s0907444904019158
发表时间:
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