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TitleStructural basis for the mechanisms of human presequence protease conformational switch and substrate recognition.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 1833, Year 2022
Publish dateApr 5, 2022
AuthorsWenguang G Liang / Juwina Wijaya / Hui Wei / Alex J Noble / Jordan M Mancl / Swansea Mo / David Lee / John V Lin King / Man Pan / Chang Liu / Carla M Koehler / Minglei Zhao / Clinton S Potter / Bridget Carragher / Sheng Li / Wei-Jen Tang /
PubMed AbstractPresequence protease (PreP), a 117 kDa mitochondrial M16C metalloprotease vital for mitochondrial proteostasis, degrades presequence peptides cleaved off from nuclear-encoded proteins and other ...Presequence protease (PreP), a 117 kDa mitochondrial M16C metalloprotease vital for mitochondrial proteostasis, degrades presequence peptides cleaved off from nuclear-encoded proteins and other aggregation-prone peptides, such as amyloid β (Aβ). PreP structures have only been determined in a closed conformation; thus, the mechanisms of substrate binding and selectivity remain elusive. Here, we leverage advanced vitrification techniques to overcome the preferential denaturation of one of two ~55 kDa homologous domains of PreP caused by air-water interface adsorption. Thereby, we elucidate cryoEM structures of three apo-PreP open states along with Aβ- and citrate synthase presequence-bound PreP at 3.3-4.6 Å resolution. Together with integrative biophysical and pharmacological approaches, these structures reveal the key stages of the PreP catalytic cycle and how the binding of substrates or PreP inhibitor drives a rigid body motion of the protein for substrate binding and catalysis. Together, our studies provide key mechanistic insights into M16C metalloproteases for future therapeutic innovations.
External linksNat Commun / PubMed:35383169 / PubMed Central
MethodsEM (single particle) / EM (tomography)
Resolution3.3 - 4.0 Å
Structure data

22278

6xos

EMDB-22278, PDB-6xos:
CryoEM structure of human presequence protease in partial open state 1
Method: EM (single particle) / Resolution: 3.7 Å

22279

6xot

EMDB-22279, PDB-6xot:
CryoEM structure of human presequence protease in partial open state 2
Method: EM (single particle) / Resolution: 3.9 Å

22280

6xou

EMDB-22280, PDB-6xou:
CryoEM structure of human presequence protease in open state
Method: EM (single particle) / Resolution: 4.0 Å

22281

6xov

EMDB-22281, PDB-6xov:
CryoEM structure of human presequence protease in partial closed state 1
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-25921:
CryoET of presequence protease single particle
Method: EM (tomography)

Source
  • homo sapiens (human)
  • Escherichia phage EcSzw-2 (virus)
KeywordsHYDROLASE / Partial open state

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