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.


2bnn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bnn.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2bnn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bnn| PDB=2bnn | SCENE= }}
{{STRUCTURE_2bnn| PDB=2bnn | SCENE= }}
-
'''STRUCTURE OF A ZN ENZYME'''
+
===STRUCTURE OF A ZN ENZYME===
-
==Overview==
+
<!--
-
The biosynthesis of fosfomycin, an oxirane antibiotic in clinical use, involves a unique epoxidation catalyzed by (S)-2-hydroxypropylphosphonic acid epoxidase (HPPE). The reaction is essentially dehydrogenation of a secondary alcohol. A high-resolution crystallographic analysis reveals that the HPPE subunit displays a two-domain combination. The C-terminal or catalytic domain has the cupin fold that binds a divalent cation, whereas the N-terminal domain carries a helix-turn-helix motif with putative DNA-binding helices positioned 34 A apart. The structure of HPPE serves as a model for numerous proteins, of ill-defined function, predicted to be transcription factors but carrying a cupin domain at the C terminus. Structure-reactivity analyses reveal conformational changes near the catalytic center driven by the presence or absence of ligand, that HPPE is a Zn(2+)/Fe(2+)-dependent epoxidase, proof that flavin mononucleotide is required for catalysis, and allow us to propose a simple mechanism that is compatible with previous experimental data. The participation of the redox inert Zn(2+) in the mechanism is surprising and indicates that Lewis acid properties of the metal ions are sufficient to polarize the substrate and, aided by flavin mononucleotide reduction, facilitate the epoxidation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16186494}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16186494 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16186494}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Epoxidase,cupin,hth,cation-dependant]]
[[Category: Epoxidase,cupin,hth,cation-dependant]]
[[Category: Zinc,fosfomycin oxidoreductase]]
[[Category: Zinc,fosfomycin oxidoreductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:32:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:45:03 2008''

Revision as of 03:45, 29 July 2008

Image:2bnn.png

Template:STRUCTURE 2bnn

STRUCTURE OF A ZN ENZYME

Template:ABSTRACT PUBMED 16186494

About this Structure

2BNN is a Single protein structure of sequence from Streptomyces wedmorensis. Full crystallographic information is available from OCA.

Reference

Structure and reactivity of hydroxypropylphosphonic acid epoxidase in fosfomycin biosynthesis by a cation- and flavin-dependent mechanism., McLuskey K, Cameron S, Hammerschmidt F, Hunter WN, Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14221-6. Epub 2005 Sep 26. PMID:16186494

Page seeded by OCA on Tue Jul 29 06:45:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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