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Titolo:
STRUCTURAL INVESTIGATION OF THE COMPLEXATION PROPERTIES BETWEEN HORSESPLEEN APOFERRITIN AND METALLOPORPHYRINS
Autore:
MICHAUX MA; DAUTANT A; GALLOIS B; GRANIER T; DESTAINTOT BL; PRECIGOUX G;
Indirizzi:
UNIV BORDEAUX 1,CRISTALLOG & PHYS CRISTALLINE LAB,ERS 133 CNRS F-33405 TALENCE FRANCE UNIV BORDEAUX 1,CRISTALLOG & PHYS CRISTALLINE LAB,ERS 133 CNRS F-33405 TALENCE FRANCE
Titolo Testata:
Proteins
fascicolo: 3, volume: 24, anno: 1996,
pagine: 314 - 321
SICI:
0887-3585(1996)24:3<314:SIOTCP>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; HEME-BINDING; LIGHT CHAIN; FERRITIN; CRYSTAL; BACTERIOFERRITIN; PURIFICATION;
Keywords:
X-RAY PROTEIN CRYSTALLOGRAPHY; STRUCTURE DETERMINATION; ANOMALOUS SCATTERING; PROTEIN-PORPHYRIN INTERACTION; METALLOPORPHYRIN DEMETALATION; MULTIPLE ALIGNMENT; STRUCTURAL COMPARISON; FERRITIN AND BACTERIOFERRITIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
M.A. Michaux et al., "STRUCTURAL INVESTIGATION OF THE COMPLEXATION PROPERTIES BETWEEN HORSESPLEEN APOFERRITIN AND METALLOPORPHYRINS", Proteins, 24(3), 1996, pp. 314-321

Abstract

Crystallographic studies of L-chain horse spleen apoferritin (HSF) co-crystallized with Pt-hematoporphyrin IX and Sn-protoporphyrin IX havebrought significant new insights into structure-function relationships in ferritins. Interactions of HSF with porphyrins are discussed. Structural results show that the nestling properties into HSF are dependent on the porphyrin moiety. (Only protoporphyrin IX significantly interacts with the protein, whereas hematoporphyrin IX does not. ) These studies additionally point out the L-chain HSF ability to demetalate metalloporphyrins, a result which is of importance in looking at the ironstorage properties of ferritins, In both compound investigated (whether the porphyrin reaches the binding site or not), the complexation appears to be concomitant with the extraction of the metal from the porphyrin. To analyze further the previous results, a three-dimensional alignment of ferritin sequences based on available crystallographic coordinates, including the present structures, is given. It confirms a high degree of homology between these members of the ferritin family and thus allows us to emphasize observed structural differences: 1) unlikeL-chain HSF, H-chain human ferritin presents no preformed binding site; and 2) despite the absence of axial ligands, and due to the demetalation, L-chain HSF is able to host protoporphyrin at a similar location to that naturally found in bacterioferritin. (C) 1996 Wiley-Liss, Inc.

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Documento generato il 28/11/20 alle ore 04:55:53