1xrl: Difference between revisions
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[[Image:1xrl.gif|left|200px]] | [[Image:1xrl.gif|left|200px]] | ||
'''Crystal structure of active site F1-mutant Y205F complex with inhibitor PCK''' | {{Structure | ||
|PDB= 1xrl |SIZE=350|CAPTION= <scene name='initialview01'>1xrl</scene>, resolution 1.82Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PHK:(2R,3S)-3-AMINO-1-CHLORO-4-PHENYL-BUTAN-2-OL'>PHK</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] | |||
|GENE= TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum]) | |||
}} | |||
'''Crystal structure of active site F1-mutant Y205F complex with inhibitor PCK''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1XRL is a [ | 1XRL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRL OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15994304 15994304] | ||
[[Category: Prolyl aminopeptidase]] | [[Category: Prolyl aminopeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: substrate recognition]] | [[Category: substrate recognition]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:13:39 2008'' | ||
Revision as of 16:13, 20 March 2008
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| , resolution 1.82Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | TA0830 (Thermoplasma acidophilum) | ||||||
| Activity: | Prolyl aminopeptidase, with EC number 3.4.11.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of active site F1-mutant Y205F complex with inhibitor PCK
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
1XRL 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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