1xrq: Difference between revisions

Revision as of 16:58, 21 February 2008

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 with as ligand. Active as Prolyl aminopeptidase, with EC number 3.4.11.5 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 Thu Feb 21 15:57:57 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1xrq.gif|left|200px]]<br /><applet load="1xrq" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1xrq.gif|left|200px]]<br /><applet load="1xrq" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1xrq, resolution 2.80&Aring;" />
 '''Crystal structure of active site F1-mutant E245Q soaked with peptide Phe-Leu'''<br />
 ==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 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 Structure==
-XRQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] with LEU as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XRQ OCA].
+XRQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum] with <scene name='pdbligand=LEU:'>LEU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRQ OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: Groll, M.]]
 [[Category: Huber, R.]]
-[[Category: Kim, J.S.]]
+[[Category: Kim, J S.]]
-[[Category: Konarev, P.V.]]
+[[Category: Konarev, P V.]]
-[[Category: Svergun, D.I.]]
+[[Category: Svergun, D I.]]
 [[Category: LEU]]
 [[Category: alpha-beta hydrolase]]
@@ Line 29: / Line 29: @@
 [[Category: substrate recognition]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:17:59 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:57 2008''