4FWG
Crystal structure of the Lon-like protease MtaLonC in complex with lactacystin
Summary for 4FWG
| Entry DOI | 10.2210/pdb4fwg/pdb |
| Related | 4FW9 4FWD 4FWH |
| Descriptor | TTC1975 peptidase, Omuralide, open form, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | lon protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Meiothermus taiwanensis |
| Total number of polymer chains | 1 |
| Total formula weight | 81377.71 |
| Authors | Chang, C.I.,Kuo, C.I.,Huang, K.F. (deposition date: 2012-07-01, release date: 2013-06-26, Last modification date: 2024-10-16) |
| Primary citation | Liao, J.H.,Ihara, K.,Kuo, C.I.,Huang, K.F.,Wakatsuki, S.,Wu, S.H.,Chang, C.I. Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors Acta Crystallogr.,Sect.D, 69:1395-1402, 2013 Cited by PubMed Abstract: The Lon proteases are a unique family of chambered proteases with a built-in AAA+ (ATPases associated with diverse cellular activities) module. Here, crystal structures of a unique member of the Lon family with no intrinsic ATPase activity in the proteolytically active form are reported both alone and in complexes with three covalent inhibitors: two peptidomimetics and one derived from a natural product. This work reveals the unique architectural features of an ATP-independent Lon that selectively degrades unfolded protein substrates. Importantly, these results provide mechanistic insights into the recognition of inhibitors and polypeptide substrates within the conserved proteolytic chamber, which may aid the development of specific Lon-protease inhibitors. PubMed: 23897463DOI: 10.1107/S0907444913008214 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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