1kv7
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1kv7.gif|left|200px]] | [[Image:1kv7.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1kv7", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | | | + | or leave the SCENE parameter empty for the default display. |
- | | | + | --> |
- | + | {{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''' | ||
Line 33: | Line 30: | ||
[[Category: Tollin, G.]] | [[Category: Tollin, G.]] | ||
[[Category: Weichsel, A.]] | [[Category: Weichsel, A.]] | ||
- | [[Category: | + | [[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 | + |
Revision as of 20:12, 2 May 2008
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 >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.
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 Fri May 2 23:12:28 2008