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.


1unb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1unb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1unb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1unb| PDB=1unb | SCENE= }}
{{STRUCTURE_1unb| PDB=1unb | SCENE= }}
-
'''DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH 2-OXOGLUTARATE AND AMPICILLIN'''
+
===DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH 2-OXOGLUTARATE AND AMPICILLIN===
-
==Overview==
+
<!--
-
Deacetoxycephalosporin-C synthase (DAOCS) is a mononuclear ferrous enzyme that transforms penicillins into cephalosporins by inserting a carbon atom into the penicillin nucleus. In the first half-reaction, dioxygen and 2-oxoglutarate produce a reactive iron-oxygen species, succinate and CO2. The oxidizing iron species subsequently reacts with penicillin to give cephalosporin and water. Here we describe high-resolution structures for ferrous DAOCS in complex with penicillins, the cephalosporin product, the cosubstrate and the coproduct. Steady-state kinetic data, quantum-chemical calculations and the new structures indicate a reaction sequence in which a 'booby-trapped' oxidizing species is formed. This species is stabilized by the negative charge of succinate on the iron. The binding sites of succinate and penicillin overlap, and when penicillin replaces succinate, it removes the stabilizing charge, eliciting oxidative attack on itself. Requisite groups of penicillin are within 1 A of the expected position of a ferryl oxygen in the enzyme-penicillin complex.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14718929}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14718929 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14718929}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Valegard, K.]]
[[Category: Valegard, K.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:27:43 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:34:41 2008''

Revision as of 11:34, 28 July 2008

Image:1unb.png

Template:STRUCTURE 1unb

DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH 2-OXOGLUTARATE AND AMPICILLIN

Template:ABSTRACT PUBMED 14718929

About this Structure

1UNB is a Single protein structure of sequence from Streptomyces clavuligerus. Full crystallographic information is available from OCA.

Reference

The structural basis of cephalosporin formation in a mononuclear ferrous enzyme., Valegard K, Terwisscha van Scheltinga AC, Dubus A, Ranghino G, Oster LM, Hajdu J, Andersson I, Nat Struct Mol Biol. 2004 Jan;11(1):95-101. Epub 2003 Dec 29. PMID:14718929

Page seeded by OCA on Mon Jul 28 14:34:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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