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1UM8

Crystal structure of helicobacter pylori ClpX

Summary for 1UM8
Entry DOI10.2210/pdb1um8/pdb
DescriptorATP-dependent Clp protease ATP-binding subunit clpX, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
Functional Keywordsclpp binding loop, chaperone
Biological sourceHelicobacter pylori
Total number of polymer chains1
Total formula weight42518.76
Authors
Kim, D.Y.,Kim, K.K. (deposition date: 2003-09-25, release date: 2003-12-23, Last modification date: 2023-12-27)
Primary citationKim, D.Y.,Kim, K.K.
Crystal Structure of ClpX Molecular Chaperone from Helicobacter pylori
J.Biol.Chem., 278:50664-50670, 2003
Cited by
PubMed Abstract: ClpX, a heat shock protein 100 chaperone, which acts as the regulatory subunit of the ATP-dependent ClpXP protease, is responsible for intracellular protein remodeling and degradation. To provide a structural basis for a better understanding of the function of the Clp ATPase family, the crystal structures of Helicobacter pylori ClpX, lacking an N-terminal Cys cluster region complexed with ADP, was determined. The overall structure of ClpX is similar to that of heat shock locus U (HslU), consisting of two subdomains, with ADP bound at the subdomain interface. The crystal structure of ClpX reveals that a conserved tripeptide (LGF) is located on the tip of ClpP binding loop extending from the N-terminal subdomain. A hexameric model of ClpX suggests that six tripeptides make hydrophobic contacts with the hydrophobic clefts of the ClpP heptmer asymmetrically. In addition, the nucleotide binding environment provides the structural explanation for the hexameric assembly and the modulation of ATPase activity.
PubMed: 14514695
DOI: 10.1074/jbc.M305882200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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