1tyf Summary

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THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS

The structure was published by Wang, J., Hartling, J.A., and Flanagan, J.M., in 1997 in a paper entitled "The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1997.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of CLP PEPTIDASE.

The most likely quaternary structure is a 14meric assembly.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
B CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
C CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
D CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
E CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
F CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
G CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
H CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
I CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
J CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
K CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
L CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
M CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%
N CLP PEPTIDASE P0A6G7 (15-207) (CLPP_ECOLI)search Escherichia coli K-12search 92% 193 94%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0A6G7 (15 - 207) CLP PEPTIDASE Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D, E, F, G, H, I, J, K, L, M, N (P0A6G7) Clp protease, ClpP subunitsearch 2-enoyl-CoA Hydratase; Chain A, domain 1search PF00574: Clp proteasesearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A, B, C, D, E, F, G, H, I, J, K, L, M, N (P0A6G7) serine-type endopeptidase activitysearch protein bindingsearch peptidase activitysearch serine-type peptidase activitysearch hydrolase activitysearch identical protein bindingsearch cytoplasmsearch cytosolsearch membranesearch proteolysissearch misfolded or incompletely synthesized protein catabolic processsearch response to temperature stimulussearch response to heatsearch

Chain InterPro annotation
A, B, C, D, E, F, G, H, I, J, K, L, M, N ATP-dependent Clp protease proteolytic subunitsearch ClpP, active sitesearch Clp protease proteolytic subunit /Translocation-enhancing protein TepAsearch ClpP/crotonase-like domainsearch