1xrq: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=LEU:LEUCINE'>LEU</scene> | |LIGAND= <scene name='pdbligand=LEU:LEUCINE'>LEU</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span> | ||
|GENE= TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum]) | |GENE= TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1mtz|1MTZ]], [[1mu0|1MU0]], [[1mt3|1MT3]], [[1xqv|1XQV]], [[1xqw|1XQW]], [[1xqx|1XQX]], [[1xqy|1XQY]], [[1xrl|1XRL]], [[1xrm|1XRM]], [[1xrn|1XRN]], [[1xro|1XRO]], [[1xrp|1XRP]], [[1xrr|1XRR]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrq OCA], [http://www.ebi.ac.uk/pdbsum/1xrq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xrq RCSB]</span> | |||
}} | }} | ||
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[[Category: Konarev, P V.]] | [[Category: Konarev, P V.]] | ||
[[Category: Svergun, D I.]] | [[Category: Svergun, D I.]] | ||
[[Category: alpha-beta hydrolase]] | [[Category: alpha-beta hydrolase]] | ||
[[Category: caged active site]] | [[Category: caged active site]] | ||
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[[Category: substrate recognition]] | [[Category: substrate recognition]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:53:44 2008'' | ||
Revision as of 00:53, 31 March 2008
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| , resolution 2.80Å | |||||||
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| Ligands: | |||||||
| Gene: | TA0830 (Thermoplasma acidophilum) | ||||||
| Activity: | Prolyl aminopeptidase, with EC number 3.4.11.5 | ||||||
| Related: | 1MTZ, 1MU0, 1MT3, 1XQV, 1XQW, 1XQX, 1XQY, 1XRL, 1XRM, 1XRN, 1XRO, 1XRP, 1XRR
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of active site F1-mutant E245Q soaked with peptide Phe-Leu
OverviewOverview
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.
About this StructureAbout this Structure
1XRQ is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
ReferenceReference
X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum., Goettig P, Brandstetter H, Groll M, Gohring W, Konarev PV, Svergun DI, Huber R, Kim JS, J Biol Chem. 2005 Sep 30;280(39):33387-96. Epub 2005 Jul 1. PMID:15994304
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