Back to Results
First PageMeta Content
Macrocycles / Microbiology / Enterobactin / Colicin / Siderophore / TonB-dependent receptors / Ferric / Transmembrane protein / Bacteriocin / Biology / Chemistry / Peripheral membrane proteins


Proc. Natl. Acad. Sci. USA Vol. 94, pp. 4560–4565, April 1997 Genetics Double mutagenesis of a positive charge cluster in the ligand-binding site of the ferric enterobactin receptor, FepA
Add to Reading List

Document Date: 2011-03-19 15:53:30


Open Document

File Size: 311,83 KB

Share Result on Facebook

City

San Francisco / Rochester / Boston / Madison / Washington / DC / Sao Paulo / Goranson / London / Norman / /

Company

Armstrong S. A. / ABC / FepA A B C D E AB / J.S.A. / Singh S. P. / SLM / AC AD AE / /

Country

United States / /

Currency

USD / /

Event

Product Issues / /

IndustryTerm

crystallographic solution / chemical interactions / chemical basis / ligand-binding site / proposed binding site / cell surface siderophore binding site / recognition site / arginine-specific chemical inactivation / colicin solutions / chemical lability / metal center / energy dependence / chemical susceptibility / chemical methods / /

Organization

Harvard Medical School / National Science Foundation / American Society for Microbiology Annual / BC BE / NATIONAL ACADEMY OF SCIENCES / AB AC / Department of Chemistry and Biochemistry / /

Person

PHILLIP E. K LEBBA / JOHN D. IGO / Chris Murphy / B. Neilands / JENNIFER S. A LLEN / Tom Ferenci / Marjorie A. Montague / Paul F. Cook / SAMUEL B. FOSTER / Leon T. Rosenberg / CATHY SPRENCEL / MARVIN A. PAYNE / /

/

Position

Dean / /

Product

mutant protein / binding / ferric enterobactin uptake / ferric enterobactin / colicin / /

ProvinceOrState

Alabama / South Dakota / S. K. / Oklahoma / Massachusetts / /

Technology

x-ray / directed mutagenesis / cloning / aeration / http / PILEUP algorithm / /

SocialTag