This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1f7z

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1f7z.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1f7z.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1f7z| PDB=1f7z | SCENE= }}
{{STRUCTURE_1f7z| PDB=1f7z | SCENE= }}
-
'''RAT TRYPSINOGEN K15A COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR'''
+
===RAT TRYPSINOGEN K15A COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR===
-
==Overview==
+
<!--
-
The contribution of induced fit to enzyme specificity has been much debated, although with little experimental data. Here we probe the effect of induced fit on enzyme specificity using the trypsin(ogen) system. BPTI is known to induce trypsinogen to assume a trypsinlike conformation. Correlations are observed between BPTI affinity and the values of k(cat)/K(m) for the hydrolysis of two substrates by eight trypsin(ogen) variants. The slope of both correlations is -1.8. The crystal structures of the BPTI complexes of four variant trypsinogens were also solved. Three of these enzymes, K15A, DeltaI16V17/D194N, and DeltaI16V17/Q156K trypsinogen, are 10- to 100-fold more active than trypsinogen. The fourth variant, DeltaI16V17 trypsinogen, is the lone outlier in the correlations; its activity is lower than expected based on its affinity for BPTI. The S1 site and oxyanion hole, formed by segments 184A-194 and 216-223, are trypsinlike in all of the enzymes. These structural and kinetic data confirm that BPTI induces an active conformation in the trypsin(ogen) variants. Thus, changes in BPTI affinity monitor changes in the energetic cost of inducing a trypsinlike conformation. Although the S1 site and oxyanion hole are similar in all four variants, the N-terminal and autolysis loop (residues 142-152) segments have different interactions for each variant. These results indicate that zymogen activity is controlled by a simple conformational equilibrium between active and inactive conformations, and that the autolysis loop and N-terminal segments control this equilibrium. Together, these data illustrate that induced fit does not generally contribute to enzyme specificity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11420435}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11420435 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11420435}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Trypsin precursor]]
[[Category: Trypsin precursor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:00:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:50:35 2008''

Revision as of 23:50, 30 June 2008

Image:1f7z.png

Template:STRUCTURE 1f7z

RAT TRYPSINOGEN K15A COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR

Template:ABSTRACT PUBMED 11420435

About this Structure

1F7Z is a Protein complex structure of sequences from Bos taurus and Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

The energetic cost of induced fit catalysis: Crystal structures of trypsinogen mutants with enhanced activity and inhibitor affinity., Pasternak A, White A, Jeffery CJ, Medina N, Cahoon M, Ringe D, Hedstrom L, Protein Sci. 2001 Jul;10(7):1331-42. PMID:11420435

Page seeded by OCA on Tue Jul 1 02:50:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f7z"
Personal tools