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.


3ubp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3ubp.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3ubp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3ubp| PDB=3ubp | SCENE= }}
{{STRUCTURE_3ubp| PDB=3ubp | SCENE= }}
-
'''DIAMIDOPHOSPHATE INHIBITED BACILLUS PASTEURII UREASE'''
+
===DIAMIDOPHOSPHATE INHIBITED BACILLUS PASTEURII UREASE===
-
==Overview==
+
<!--
-
BACKGROUND: Urease catalyzes the hydrolysis of urea, the final step of organic nitrogen mineralization, using a bimetallic nickel centre. The role of the active site metal ions and amino acid residues has not been elucidated to date. Many pathologies are associated with the activity of ureolytic bacteria, and the efficiency of soil nitrogen fertilization with urea is severely decreased by urease activity. Therefore, the development of urease inhibitors would lead to a reduction of environmental pollution, to enhanced efficiency of nitrogen uptake by plants, and to improved therapeutic strategies for treatment of infections due to ureolytic bacteria. Structure-based design of urease inhibitors would require knowledge of the enzyme mechanism at the molecular level. RESULTS: The structures of native and inhibited urease from Bacillus pasteurii have been determined at a resolution of 2.0 A by synchrotron X-ray cryogenic crystallography. In the native enzyme, the coordination sphere of each of the two nickel ions is completed by a water molecule and a bridging hydroxide. A fourth water molecule completes a tetrahedral cluster of solvent molecules. The enzyme crystallized in the presence of phenylphosphorodiamidate contains the tetrahedral transition-state analogue diamidophosphoric acid, bound to the two nickel ions in an unprecedented mode. Comparison of the native and inhibited structures reveals two distinct conformations of the flap lining the active-site cavity. CONCLUSIONS: The mode of binding of the inhibitor, and a comparison between the native and inhibited urease structures, indicate a novel mechanism for enzymatic urea hydrolysis which reconciles the available structural and biochemical data.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10368287}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10368287 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10368287}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Nickel]]
[[Category: Nickel]]
[[Category: Urease]]
[[Category: Urease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:14:54 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:10:49 2008''

Revision as of 10:10, 3 July 2008

Image:3ubp.png

Template:STRUCTURE 3ubp

DIAMIDOPHOSPHATE INHIBITED BACILLUS PASTEURII UREASE

Template:ABSTRACT PUBMED 10368287

About this Structure

3UBP is a Protein complex structure of sequences from Sporosarcina pasteurii. Full crystallographic information is available from OCA.

Reference

A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels., Benini S, Rypniewski WR, Wilson KS, Miletti S, Ciurli S, Mangani S, Structure. 1999 Feb 15;7(2):205-16. PMID:10368287

Page seeded by OCA on Thu Jul 3 13:10:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ubp"
Personal tools