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Science 18 December 1998: Vol. 282. no. 5397, pp. 2202 - 2203 DOI: 10.1126/science.282.5397.2202
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Perspectives
PROTEIN STRUCTURE: Pumping Iron Through Cell Membranes
Volkmar Braun
Despite their importance in various cellular functions, the three-dimensional structure at atomic resolution has been determined for only a few membrane proteins. In his Perspective, Braun discusses results reported in the same issue by Ferguson et al. in which the crystal structure of FhuA, an iron transporter protein, has been determined at high resolution. This and related proteins may be the general model for a large class of iron-transporting molecules.
The author is in the department of Mikrobiologie/Membranphysiologie, Universität Tüebingen, D-72076 Tübingen, Germany. E-mail: volkmar.braun{at}mikrobio.uni-tuebingen.de
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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
- The Ton System, an ABC Transporter, and a Universally Conserved GTPase Are Involved in Iron Utilization by Brucella melitensis 16M.
- I. Danese, V. Haine, R.-M. Delrue, A. Tibor, P. Lestrate, O. Stevaux, P. Mertens, J.-Y. Paquet, J. Godfroid, X. De Bolle, et al. (2004)
Infect. Immun.
72, 5783-5790
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- TonB of Escherichia coli activates FhuA through interaction with the {beta}-barrel.
- H. Killmann, C. Herrmann, A. Torun, G. Jung, and V. Braun (2002)
Microbiology
148, 3497-3509
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- Microbial iron transport via a siderophore shuttle: A membrane ion transport paradigm.
- A. Stintzi, C. Barnes, J. Xu, and K. N. Raymond (2000)
PNAS
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- An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis.
- S. K. Mazmanian, H. Ton-That, K. Su, and O. Schneewind (2002)
PNAS
99, 2293-2298
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- Microbial iron transport via a siderophore shuttle: A membrane ion transport paradigm.
- A. Stintzi, C. Barnes, J. Xu, and K. N. Raymond (2000)
PNAS
97, 10691-10696
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