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.


1kv7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kv7.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1kv7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kv7| PDB=1kv7 | SCENE= }}
{{STRUCTURE_1kv7| PDB=1kv7 | SCENE= }}
-
'''Crystal Structure of CueO, a multi-copper oxidase from E. coli involved in copper homeostasis'''
+
===Crystal Structure of CueO, a multi-copper oxidase from E. coli involved in copper homeostasis===
-
==Overview==
+
<!--
-
CueO (YacK), a multicopper oxidase, is part of the copper-regulatory cue operon in Escherichia coli. The crystal structure of CueO has been determined to 1.4-A resolution by using multiple anomalous dispersion phasing and an automated building procedure that yielded a nearly complete model without manual intervention. This is the highest resolution multicopper oxidase structure yet determined and provides a particularly clear view of the four coppers at the catalytic center. The overall structure is similar to those of laccase and ascorbate oxidase, but contains an extra 42-residue insert in domain 3 that includes 14 methionines, nine of which lie in a helix that covers the entrance to the type I (T1, blue) copper site. The trinuclear copper cluster has a conformation not previously seen: the Cu-O-Cu binuclear species is nearly linear (Cu-O-Cu bond angle = 170 degrees) and the third (type II) copper lies only 3.1 A from the bridging oxygen. CueO activity was maximal at pH 6.5 and in the presence of &gt;100 microM Cu(II). Measurements of intermolecular and intramolecular electron transfer with laser flash photolysis in the absence of Cu(II) show that, in addition to the normal reduction of the T1 copper, which occurs with a slow rate (k = 4 x 10(7) M(-1)x (-1)), a second electron transfer process occurs to an unknown site, possibly the trinuclear cluster, with k = 9 x 10(7) M(-1) x (-1), followed by a slow intramolecular electron transfer to T1 copper (k approximately 10 s(-1)). These results suggest the methionine-rich helix blocks access to the T1 site in the absence of excess copper.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11867755}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11867755 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11867755}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Weichsel, A.]]
[[Category: Weichsel, A.]]
[[Category: Multi-copper oxidase]]
[[Category: Multi-copper oxidase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:12:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:04:24 2008''

Revision as of 08:04, 2 July 2008

Image:1kv7.png

Template:STRUCTURE 1kv7

Crystal Structure of CueO, a multi-copper oxidase from E. coli involved in copper homeostasis

Template:ABSTRACT PUBMED 11867755

About this Structure

1KV7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli., Roberts SA, Weichsel A, Grass G, Thakali K, Hazzard JT, Tollin G, Rensing C, Montfort WR, Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2766-71. Epub 2002 Feb 26. PMID:11867755

Page seeded by OCA on Wed Jul 2 11:04:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kv7"
Personal tools