1um8 | pdb_00001um8
Crystal structure of helicobacter pylori ClpX
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Overview
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.
About this Structure
1UM8 is a Single protein structure of sequence from Helicobacter pylori 26695 with ADP as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of ClpX molecular chaperone from Helicobacter pylori., Kim DY, Kim KK, J Biol Chem. 2003 Dec 12;278(50):50664-70. Epub 2003 Sep 26. PMID:14514695
Page seeded by OCA on Wed Nov 21 04:14:17 2007
