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Molecular dynamics simulations of the bacterial outer membrane protein FhuA: a comparative study of the ferrichrome-free and bound states.

Abstract:

FhuA is one of the more complex members of the superfamily of bacterial outer membrane proteins. Its primary function is to provide a binding site on the outer membrane surface for siderophores, such as ferrichrome, and subsequently to facilitate their energy-dependent transport across the membrane, presumably powered by the TonB-ExbBD protein complex that resides in the cytoplasmic membrane. Crystal structures of FhuA with and without a bound ferrichrome molecule have provided some clues as ...

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Publication status:
Published

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Authors


Faraldo-Gómez, JD More by this author
Sansom, MS More by this author
Journal:
Biophysical journal
Volume:
85
Issue:
3
Pages:
1406-1420
Publication date:
2003-09-05
DOI:
EISSN:
1542-0086
ISSN:
0006-3495
URN:
uuid:113745fb-f040-456e-9d06-ea4fec5d7aaa
Source identifiers:
100690
Local pid:
pubs:100690

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