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.


2ik4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ik4.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2ik4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ik4| PDB=2ik4 | SCENE= }}
{{STRUCTURE_2ik4| PDB=2ik4 | SCENE= }}
-
'''Yeast inorganic pyrophosphatase variant D117E with magnesium and phosphate'''
+
===Yeast inorganic pyrophosphatase variant D117E with magnesium and phosphate===
-
==Overview==
+
<!--
-
We have determined the structures of the wild type and seven active site variants of yeast inorganic pyrophosphatase (PPase) in the presence of Mg2+ and phosphate, providing the first complete structural description of its catalytic cycle. PPases catalyze the hydrolysis of pyrophosphate and require four divalent metal cations for catalysis; magnesium provides the highest activity. The crystal form chosen contains two monomers in the asymmetric unit, corresponding to distinct catalytic intermediates. In the "closed" wild-type active site, one of the two product phosphates has already dissociated, while the D115E variant "open" conformation is of the hitherto unobserved two-phosphate and two-"bridging" water active site. The mutations affect metal binding and the hydrogen bonding network in the active site, allowing us to explain the effects of mutations. For instance, in Y93F, F93 binds in a cryptic hydrophobic pocket in the absence of substrate, preserving hydrogen bonding in the active site and leading to relatively small changes in solution properties. This is not true in the presence of substrate, when F93 is forced back into the active site. Such subtle changes underline how low the energy barriers are between thermodynamically favorable conformations of the enzyme. The structures also allow us to associate metal binding constants to specific sites. Finally, the wild type and the D152E variant contain a phosphate ion adjacent to the active site, showing for the first time how product is released through a channel of flexible cationic side chains.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17260952}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17260952 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17260952}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Structure-function]]
[[Category: Structure-function]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:35:44 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:17:19 2008''

Revision as of 20:17, 27 July 2008

Image:2ik4.png

Template:STRUCTURE 2ik4

Yeast inorganic pyrophosphatase variant D117E with magnesium and phosphate

Template:ABSTRACT PUBMED 17260952

About this Structure

2IK4 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

A complete structural description of the catalytic cycle of yeast pyrophosphatase., Oksanen E, Ahonen AK, Tuominen H, Tuominen V, Lahti R, Goldman A, Heikinheimo P, Biochemistry. 2007 Feb 6;46(5):1228-39. PMID:17260952

Page seeded by OCA on Sun Jul 27 23:17:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ik4"
Personal tools