1xro

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[[Image:1xro.gif|left|200px]]<br /><applet load="1xro" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xro.gif|left|200px]]
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caption="1xro, resolution 1.80&Aring;" />
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'''Crystal structure of active site F1-mutant E213Q soaked with peptide Phe-Leu'''<br />
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{{Structure
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|PDB= 1xro |SIZE=350|CAPTION= <scene name='initialview01'>1xro</scene>, resolution 1.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=LEU:LEUCINE'>LEU</scene>
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|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]
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|GENE= TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum])
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}}
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'''Crystal structure of active site F1-mutant E213Q soaked with peptide Phe-Leu'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1XRO 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=1XRO OCA].
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1XRO 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=1XRO OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15994304 15994304]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:13:43 2008''

Revision as of 13:13, 20 March 2008

Image:1xro.gif


PDB ID 1xro

Drag the structure with the mouse to rotate
, resolution 1.80Å
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 E213Q soaked with peptide Phe-Leu


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.

About this Structure

1XRO is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.

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:15994304

Page seeded by OCA on Thu Mar 20 15:13:43 2008

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