Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1XQW

Crystal structure of F1-mutant S105A complex with PHE-LEU

Summary for 1XQW
Entry DOI10.2210/pdb1xqw/pdb
Related1MT3 1MTZ 1MU0 1XQV 1XQX 1XQY
DescriptorProline iminopeptidase, PHENYLALANINE, LEUCINE, ... (4 entities in total)
Functional Keywordsalpha-beta hydrolase, caged active site, catalytic triad, nucleophile, hydrolase
Biological sourceThermoplasma acidophilum
Total number of polymer chains1
Total formula weight34106.81
Authors
Goettig, P.,Brandstetter, H.,Groll, M.,Goehring, W.,Konarev, P.V.,Svergun, D.I.,Huber, R.,Kim, J.-S. (deposition date: 2004-10-13, release date: 2005-07-12, Last modification date: 2024-10-09)
Primary citationGoettig, P.,Brandstetter, H.,Groll, M.,Goehring, W.,Konarev, P.V.,Svergun, D.I.,Huber, R.,Kim, J.-S.
X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum
J.Biol.Chem., 280:33387-33396, 2005
Cited by
PubMed Abstract: The tricorn-interacting factor F1 of the archaeon Thermoplasma acidophilum cleaves small hydrophobic peptide products of the proteasome and tricorn protease. F1 mutants of the active site residues that are involved in substrate recognition and catalysis displayed distinct activity patterns toward fluorogenic test substrates. Crystal structures of the mutant proteins complexed with peptides Phe-Leu, Pro-Pro, or Pro-Leu-Gly-Gly showed interaction of glutamates 213 and 245 with the N termini of the peptides and defined the S1 and S1' sites and the role of the catalytic residues. Evidence was found for processive peptide cleavage in the N-to-C direction, whereby the P1' product is translocated into the S1 site. A functional interaction of F1 with the tricorn protease was observed with the inactive F1 mutant G37A. Moreover, small angle x-ray scattering measurements for tricorn and inhibited F1 have been interpreted as formation of transient and substrate-induced complexes.
PubMed: 15994304
DOI: 10.1074/jbc.M505030200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

227933

PDB entries from 2024-11-27

PDB statisticsPDBj update infoContact PDBjnumon