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TitleSmall molecule dysregulation of ClpP activity via bidirectional allosteric pathways.
Journal, issue, pagesStructure, Vol. 33, Page 1700-, Year 2025
Publish dateDec 16, 2024 (structure data deposition date)
AuthorsBarghash, M.M. / Mabanglo, M.F. / Hoff, S.E. / Brozdnychenko, D. / Wong, K.S. / Binepal, G. / Ip, P. / Shen, J. / Furukawa, T. / Katayama, H. ...Barghash, M.M. / Mabanglo, M.F. / Hoff, S.E. / Brozdnychenko, D. / Wong, K.S. / Binepal, G. / Ip, P. / Shen, J. / Furukawa, T. / Katayama, H. / Trudel, V. / Tan, J. / Yudin, A.K. / Gray-Owen, S.D. / Sakuda, S. / Batey, R.A. / Vahidi, S. / Bonomi, M. / Houry, W.A.
External linksStructure / PubMed:40795847
MethodsX-ray diffraction
Resolution1.9 - 1.99 Å
Structure data

PDB-9mjp:
Crystal structure of Neisseria meningitidis ClpP protease complex with boronate compound BC8a
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

PDB-9mk2:
Crystal structure of Neisseria meningitidis ClpP protease complex with noncovalent activator, ACP1-01
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-9mk5:
Crystal structure of Neisseria meningitidis ClpP protease complex with small molecule activator, Dioctatin
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-JT7:
N-[(1R)-1-borono-3-methylbutyl]-N~2~-(2-chloro-4-methoxybenzene-1-carbonyl)-L-leucinamide

ChemComp-HOH:
WATER

PDB-1blz:
ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACV-FE-NO COMPLEX)

PDB-1bmh:
Unknown entry

Source
  • neisseria meningitidis (bacteria)
KeywordsHYDROLASE / boronate / covalent / inhibitor / activator / noncovalent / agonist / allosteric / small molecule / metabolite

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