We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1n6f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1n6f.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1n6f.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1n6f| PDB=1n6f | SCENE= }}
{{STRUCTURE_1n6f| PDB=1n6f | SCENE= }}
-
'''tricorn protease in complex with Z-Phe-diketo-Arg-Glu-Phe'''
+
===tricorn protease in complex with Z-Phe-diketo-Arg-Glu-Phe===
-
==Overview==
+
<!--
-
The proposed pathway and mechanism of substrate entry and product egress in the hexameric D3 symmetric tricorn protease from Thermoplasma acidophilum were explored by crystallographic studies of ligand complexes and by structure-based mutagenesis. Obstruction of the pore within the 7-bladed beta-propeller (beta7) domain by alkylation or oxidation of an engineered double cysteine mutant strongly decreased enzymatic activities. In line herewith, the crystal structure of the tricorn protease in complex with a trideca-peptide inhibitor modifying the catalytic Ser965 revealed part of the peptide trapped inside the channel of the beta7 domain. The cysteine mutation widening the lumen of the 6-bladed beta-propeller (beta6) domain enhanced catalytic activity, which was restored to normal values after its alkylation. A charge reversal mutant at the putative anchor site of the substrate C terminus, R131E-R132E, drastically reduced the proteolytic activity. The complex crystal structure of a peptide inhibitor with a diketo group at the cleavage site mapped the substrate recognition site and confirmed the role of Arg131-Arg132 as an anchor site. Our results strongly suggest the wider beta7 domain to serve as a selective filter and guide of the substrate to the sequestered active site, while the narrower beta6 domain routes the product to the surface. Moreover, we identified the role of Arg131-Arg132 in anchoring the substrate C terminus.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12470958}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12470958 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12470958}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Propeller]]
[[Category: Propeller]]
[[Category: Tricorn protease]]
[[Category: Tricorn protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:09:23 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:56:56 2008''

Revision as of 05:57, 29 July 2008

Image:1n6f.png

Template:STRUCTURE 1n6f

tricorn protease in complex with Z-Phe-diketo-Arg-Glu-Phe

Template:ABSTRACT PUBMED 12470958

About this Structure

1N6F is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.

Reference

Navigation inside a protease: substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum., Kim JS, Groll M, Musiol HJ, Behrendt R, Kaiser M, Moroder L, Huber R, Brandstetter H, J Mol Biol. 2002 Dec 13;324(5):1041-50. PMID:12470958

Page seeded by OCA on Tue Jul 29 08:56:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n6f"
Personal tools