1xrm: Difference between revisions

Revision as of 00:11, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1xrm.png

Template:STRUCTURE 1xrm

Crystal structure of active site F1-mutant E213Q soaked with peptide Ala-PheCrystal structure of active site F1-mutant E213Q soaked with peptide Ala-Phe

Template:ABSTRACT PUBMED 15994304

About this StructureAbout this Structure

1XRM 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

Page seeded by OCA on Mon Jul 28 00:11:42 2008

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OCA

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-'''Crystal structure of active site F1-mutant E213Q soaked with peptide Ala-Phe'''
+===Crystal structure of active site F1-mutant E213Q soaked with peptide Ala-Phe===
-==Overview==
+<!--
-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
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 [[Category: Peptide cleavage]]
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