How to Advertise
Home | This Week's Contents  |  C&EN ClassifiedsSearch C&EN Online

Millennium Special Report
C&EN 75th Anniversary Issue
Related Person
Amy C. Rosenzweig
E-mail this article to a friend
Print this article
E-mail the editor
 Table of Contents
 C&EN Classifieds
 News of the Week
 Cover Story
 Editor's Page
 Government & Policy
  Government & Policy
 ACS News
 Digital Briefs
 ACS Comments
 Career & Employment
 Special Reports
 What's That Stuff?
 Pharmaceutical Century

 Hot Articles
 Safety  Letters

 Back Issues

 How to Subscribe
 Subscription Changes
 About C&EN
 Copyright Permission
 E-mail webmaster
September 10, 2001
Volume 79, Number 37
CENEAR 79 37 p. 11
ISSN 0009-2347
[Previous Story] [Next Story]

Metal Chaperones At Work


Chemists at Northwestern University have captured the first snapshot of a metallochaperone protein at work. Audrey L. Lamb, a postdoctoral researcher in the laboratory of assistant professor Amy C. Rosenzweig, and colleagues have determined the X-ray structure of a chaperone protein that transports copper, complexed with its target enzyme, a superoxide dismutase called SOD1 [Nat. Struct. Biol., 8, 751 (2001)].

HANDSHAKE Subunit of the enzyme SOD1, purple, joins with subunit from copper chaperone protein, whose various domains are shown in blue, green, and yellow.
"We have the first image of a structure that delivers copper to its target," Lamb says.

One-third of all known proteins contain metal cofactors that are almost always essential for the catalytic function of the enzyme. Yet little is known about how these often very reactive metals are transported within cells and inserted properly into the appropriate proteins.

In the case of the copper chaperone protein and SOD1, the Northwestern chemists find, both the chaperone and the target proteins ordinarily exist as dimers of identical subunits, and the interface between these two subunits is very similar in both proteins. The transfer complex contains one subunit from each protein.

The complex structure "shows how these two proteins recognize each other, and it goes a long way toward explaining how the actual transfer of the metal ion might take place," Rosenzweig explains. Joining similarly shaped subunits from a chaperone protein and a target may be a general route for transferring metals from one protein to another, she suggests.

"The findings are truly groundbreaking," says Valeria L. Culotta, professor of environmental health sciences at Johns Hopkins University. They provide "new insight--in remarkable detail--into a metal transfer mechanism."

[Previous Story] [Next Story]


Chemical & Engineering News
Copyright © 2001 American Chemical Society

How to Advertise
Home | Table of Contents | News of the Week | Cover Story
Business | Government & Policy | Science/Technology
Chemical & Engineering News
Copyright © 2001 American Chemical Society - All Right Reserved
1155 16th Street NW • Washington DC 20036 • (202) 872-4600 • (800) 227-5558

CASChemPortChemCenterPubs Page