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Titolo:
CRYSTAL-STRUCTURE OF METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE,PYROCOCCUS-FURIOSUS
Autore:
TAHIROV TH; OKI H; TSUKIHARA T; OGASAHARA K; YUTANI K; OGATA K; IZU Y; TSUNASAWA S; KATO I;
Indirizzi:
OSAKA UNIV,INST PROT RES,3-2 YAMADAOKA SUITA OSAKA 565 JAPAN OSAKA UNIV,INST PROT RES SUITA OSAKA 565 JAPAN KANAGAWA ACAD SCI & TECHNOL,KANAZAWA KU YOKOHAMA KANAGAWA 236 JAPAN YOKOHAMA CITY UNIV,SCH MED,DEPT BIOL STRUCT,KANAZAWA KU YOKOHAMA KANAGAWA 236 JAPAN TAKARA SHUZO CO LTD,BIOMED GRP OTSU SHIGA 52021 JAPAN
Titolo Testata:
Journal of Molecular Biology
fascicolo: 1, volume: 284, anno: 1998,
pagine: 101 - 124
SICI:
0022-2836(1998)284:1<101:COMAFH>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
LENS LEUCINE AMINOPEPTIDASE; X-RAY; ESCHERICHIA-COLI; ANGSTROM RESOLUTION; SACCHAROMYCES-CEREVISIAE; THERMOTOGA-MARITIMA; MOLECULAR-CLONING; PROTEIN STABILITY; HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE;
Keywords:
HYPERTHERMOPHILE; METHIONINE AMINOPEPTIDASE; COBALT-DEPENDENT ENZYME; WATER-MEDIATED CRYSTAL TRANSFORMATION; BINUCLEAR REACTION CENTER;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
101
Recensione:
Indirizzi per estratti:
Citazione:
T.H. Tahirov et al., "CRYSTAL-STRUCTURE OF METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE,PYROCOCCUS-FURIOSUS", Journal of Molecular Biology, 284(1), 1998, pp. 101-124

Abstract

The structure of methionine aminopeptidase from hyperthermophile Pyrococcus furiosus (PfMAP) with an optimal growth temperature of 100 degrees C was determined by the multiple isomorphous replacement method and refined in three different crystal forms, one monoclinic and two hexagonal, at resolutions of 2.8, 2.9, and 3.5 Angstrom. The resolution of the monoclinic crystal form was extended to 1.75 Angstrom by water-mediated transformation to a low-humidity form, and the obtained diffraction data used for high-resolution structure refinement. This is the first description of a eukaryotic type methionine aminopeptidase structure. The PfMAP molecule is composed of two domains, a catalytic domain and an insertion domain, connected ain two antiparallel beta-strands. The catalytic domain, which possesses an internal 2-fold symmetry and contains two cobalt ions in the active site, resembles the structureof a prokaryotic type MAP from Escherichia coli (EcMAP), while the structure of the insertion domain containing three helices has a novel fold and accounts for a major difference between the eukaryotic and prokaryotic types of methionine aminopeptidase. Analysis of the PfMAP structure in comparison with EcMAP and other mesophile proteins reveals several factors which may contribute to the hyperthermostability of PFMAP: (1) a significantly high number of hydrogen bonds and ion-pairs between side-chains of oppositely charged residues involved in the stabilization of helices; (2) an increased number of hydrogen bonds betweenthe positively charged side-chain and neutral oxygen; (3) a larger number of buried water molecules involved in crosslinking the backbone atoms of sequentially separate segments; (4) stabilization of hive antiparallel P-strands connecting the two domains of the molecule by proline residues; (5) shortening of N and C-terminal tails and stabilization of the loop c(3)E by deletion of three residues. (C) 1998 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 07:31:53