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Titolo:
SHUFFLING OF STRUCTURAL ELEMENTS IN FILAMENTOUS BACTERIOPHAGES
Autore:
KISHCHENKO G; MAKOWSKI L;
Indirizzi:
FLORIDA STATE UNIV,INST MOL BIOPHYS TALLAHASSEE FL 32306 FLORIDA STATE UNIV,INST MOL BIOPHYS TALLAHASSEE FL 32306
Titolo Testata:
Proteins
fascicolo: 3, volume: 27, anno: 1997,
pagine: 405 - 409
SICI:
0887-3585(1997)27:3<405:SOSEIF>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
PFL COAT PROTEIN; VIRUS STRUCTURE; DYNAMICS; SURFACE; DNA;
Keywords:
CLASS II FILAMENTOUS BACTERIOPHAGES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
18
Recensione:
Indirizzi per estratti:
Citazione:
G. Kishchenko e L. Makowski, "SHUFFLING OF STRUCTURAL ELEMENTS IN FILAMENTOUS BACTERIOPHAGES", Proteins, 27(3), 1997, pp. 405-409

Abstract

All class II filamentous bacteriophage coat proteins contain a conserved, la-amino acid sequence highly homologous to the loop portion of the EF-hand Ca2+-binding motif. The Pf3 coat protein contains two regions of homology to this sequence, The 12-amino acid sequence corresponds to a region of the Pf1 coat protein whose structure is controversial, In some models of the virus structure, this region is alpha-helical. In others, it forms a loop that folds back on itself, The similarity of this region to the loop in the helix-loop-helix Ca2+-binding motif suggests that it takes on a loop structure in the virion, Each filamentous phage lacks at least one residue normally involved in Ca2+-coordination, consistent with the relatively weak Ca2+ binding properties ofthe filamentous phages. Consideration of the structure of the coat protein in the membrane and in the virus particle indicates that the protein may be more effective in binding cations in its membrane-bound form than in the virus particle. This suggests that release of cations from this loop may be an obligate step during assembly of the proteins into the virus particle. (C) 1997 Wiley-Liss, Inc.

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Documento generato il 01/12/20 alle ore 10:10:41