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Structure paper

TitleStructural Basis for the Magnesium-Dependent Activation and Hexamerization of the Lon AAA+ Protease.
Journal, issue, pagesStructure, Vol. 24, Issue 5, Page 676-686, Year 2016
Publish dateMay 3, 2016
AuthorsShih-Chieh Su / Chien-Chu Lin / Hui-Chung Tai / Mu-Yueh Chang / Meng-Ru Ho / C Satheesan Babu / Jiahn-Haur Liao / Shih-Hsiung Wu / Yuan-Chih Chang / Carmay Lim / Chung-I Chang /
PubMed AbstractThe Lon AAA+ protease (LonA) plays important roles in protein homeostasis and regulation of diverse biological processes. LonA behaves as a homomeric hexamer in the presence of magnesium (Mg(2+)) and ...The Lon AAA+ protease (LonA) plays important roles in protein homeostasis and regulation of diverse biological processes. LonA behaves as a homomeric hexamer in the presence of magnesium (Mg(2+)) and performs ATP-dependent proteolysis. However, it is also found that LonA can carry out Mg(2+)-dependent degradation of unfolded protein substrate in an ATP-independent manner. Here we show that in the presence of Mg(2+) LonA forms a non-secluded hexameric barrel with prominent openings, which explains why Mg(2+)-activated LonA can operate as a diffusion-based chambered protease to degrade unstructured protein and peptide substrates efficiently in the absence of ATP. A 1.85 Å crystal structure of Mg(2+)-activated protease domain reveals Mg(2+)-dependent remodeling of a substrate-binding loop and a potential metal-binding site near the Ser-Lys catalytic dyad, supported by biophysical binding assays and molecular dynamics simulations. Together, these findings reveal the specific roles of Mg(2+) in the molecular assembly and activation of LonA.
External linksStructure / PubMed:27041593
MethodsEM (single particle) / X-ray diffraction
Resolution1.85 - 12.6 Å
Structure data

EMDB-6303:
The cryo-EM structure of Meiothermus taiwanensis Lon protease with Mg2+
Method: EM (single particle) / Resolution: 12.6 Å

EMDB-6305:
The cryo-EM structure of Meiothermus taiwanensis Lon protease with ATP and Mg2+
Method: EM (single particle) / Resolution: 11.8 Å

PDB-4ypm:
Crystal structure of a LonA protease domain in complex with bortezomib
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-5e7s:
Hexameric structure of a LonA protease domain in active state
Method: X-RAY DIFFRACTION / Resolution: 3.03 Å

Chemicals

ChemComp-BO2:
N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE / medication, anticancer*YM / Bortezomib

ChemComp-MG:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER / Diethylene glycol

ChemComp-CIT:
CITRIC ACID / Citric acid

ChemComp-HOH:
WATER / Water

Source
  • meiothermus taiwanensis (bacteria)
KeywordsHYDROLASE / AAA+ domain / Lon protease / protease domain / Magnesium / Bortezomib

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