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| [[Image:1xrq.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1xrq| PDB=1xrq | SCENE= }} | | {{STRUCTURE_1xrq| PDB=1xrq | SCENE= }} |
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| '''Crystal structure of active site F1-mutant E245Q soaked with peptide Phe-Leu'''
| | ===Crystal structure of active site F1-mutant E245Q soaked with peptide Phe-Leu=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_15994304}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15994304 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15994304}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Peptide cleavage]] | | [[Category: Peptide cleavage]] |
| [[Category: Substrate recognition]] | | [[Category: Substrate recognition]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:25:36 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:31:16 2008'' |