Synergistic anion and metal binding to the ferric ion-binding protein from Neisseria gonorrhoeae

Journal of Biological Chemistry

Volumn 278, Issue 4, 2003, Pages 2490-2502

  Guo, Maolin ^a,e   Harvey, Ian ^b   Yang, Weiping ^a,e   Coghill, Lorraine ^a   Campopiano, Dominic J ^a   Parkinson, John A ^a   MacGillivray, Ross T A ^c   Harris, Wesley R ^d   Sadler, Peter J ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

^b DARESBURY LABORATORY   (United Kingdom)

^c UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^d UNIVERSITY OF MISSOURI ST LOUIS   (United States)

^e UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHARGE TRANSFER; CRYSTALLOGRAPHY; HYDROGEN BONDS; NEGATIVE IONS; OXIDATION;

LIGANDS;

PROTEINS;

ANION; BISMUTH; COBALT; FERRIC ION; FERRIC ION BINDING PROTEIN; GALLIUM; IRON; IRON BINDING PROTEIN; LIGAND; METAL ION; NITRILOTRIACETIC ACID; OXALIC ACID; PYROPHOSPHATE; TRANSFERRIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CATION TRANSPORT PROTEIN; FBPC PROTEIN, NEISSERIA GONORRHOEAE; IRON TRANSPORT PROTEIN, NEISSERIA GONORRHOEAE; IRON-TRANSPORT PROTEIN, NEISSERIA GONORRHOEAE; METAL;

ARTICLE; BINDING SITE; GENE OVEREXPRESSION; IRON STORAGE; IRON TRANSPORT; MASS SPECTROMETRY; METAL BINDING; NEISSERIA; NEISSERIA GONORRHOEAE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN PURIFICATION; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ESCHERICHIA COLI; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR CLONING; PH; PROTEIN BINDING; RADIATION SCATTERING; SPECTROPHOTOMETRY; ULTRAVIOLET RADIATION; X RAY;

NEISSERIA; NEISSERIA GONORRHOEAE;

ANIONS; BACTERIAL PROTEINS; CATION TRANSPORT PROTEINS; CLONING, MOLECULAR; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MASS SPECTROMETRY; METALS; MODELS, CHEMICAL; MODELS, MOLECULAR; NEISSERIA GONORRHOEAE; PROTEIN BINDING; SCATTERING, RADIATION; SPECTROPHOTOMETRY; TRANSFERRIN; ULTRAVIOLET RAYS; X-RAYS;

EID: 0037462639     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M208776200     Document Type: Article

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