Information Services banner Edinburgh Research Archive The University of Edinburgh crest

Edinburgh Research Archive >
Chemistry, School of >
Chemistry publications >

Please use this identifier to cite or link to this item: http://hdl.handle.net/1842/661

This item has been viewed 5 times in the last year. View Statistics

Files in This Item:

File Description SizeFormat
Campopiano_1.pdf262.97 kBAdobe PDFView/Open
Title: Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif
Authors: Zhu, Haizhong
Alexeev, Dmitriy
Hunter, Dominic JB
Campopiano, Dominic J
Sadler, Peter J
Issue Date: 2003
Citation: Biochemical Journal (2003), 376(1), 35-41
Publisher: Portland Press
Abstract: We report a set of three 1.8–1.9 Å resolution X-ray crystal structures of Neisseria gonorrhoeae Fbp (ferric-ion binding protein): (i) open-cleft apo-Fbp containing bound phosphate, (ii) opencleft mono-Fe Fbp capped by nitrilotriacetate, and (iii) open-cleft trinuclear oxo-iron Fbp, the first structure of an iron-cluster adduct of a transferrin. The nine independent molecules in the unit cells provide ‘snapshots’ of the versatile dynamic structural roles of the conserved dityrosyl iron-binding motif (Tyr195-Tyr196) which control the capture and, possibly, processing of iron. These findings have implications for understanding bacterial iron acquisition and dissimilation, and organic/mineral interfaces. Key words: bacterial transferrin, dityrosyl motif, iron-binding protein, iron transport, oxo-iron cluster, X-ray crystallography.
Keywords: Bacterial Transferrin
Dityrosyl motif
iron-binding protein
iron transport
oxo-iron cluster
x-ray crystallography
URI: http://hdl.handle.net/1842/661
Appears in Collections:Chemistry publications

Items in ERA are protected by copyright, with all rights reserved, unless otherwise indicated.

 

Valid XHTML 1.0! Unless explicitly stated otherwise, all material is copyright © The University of Edinburgh 2013, and/or the original authors. Privacy and Cookies Policy