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Titolo:
SOLUTION STRUCTURE OF THE ACTINORHODIN POLYKETIDE SYNTHASE ACYL CARRIER PROTEIN FROM STREPTOMYCES-COELICOLOR A3(2)
Autore:
CRUMP MP; CROSBY J; DEMPSEY CE; PARKINSON JA; MURRAY M; HOPWOOD DA; SIMPSON TJ;
Indirizzi:
UNIV BRISTOL,MOL RECOGNIT CTR,SCH CHEM,CANTOCKS CLOSE BRISTOL BS8 1TSAVON ENGLAND UNIV BRISTOL,MOL RECOGNIT CTR,SCH CHEM BRISTOL BS8 1TS AVON ENGLAND UNIV BRISTOL,MOL RECOGNIT CTR,DEPT BIOCHEM BRISTOL BS8 1TD AVON ENGLAND UNIV EDINBURGH,DEPT CHEM,ULTRA HIGH FIELD NMR CTR EDINBURGH EH9 3JJ MIDLOTHIAN SCOTLAND JOHN INNES CTR PLANT SCI RES NORWICH NR4 7UH NORFOLK ENGLAND
Titolo Testata:
Biochemistry
fascicolo: 20, volume: 36, anno: 1997,
pagine: 6000 - 6008
SICI:
0006-2960(1997)36:20<6000:SSOTAP>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; FATTY-ACID BIOSYNTHESIS; TWO-DIMENSIONAL H-1-NMR; ENGINEERED BIOSYNTHESIS; 3-DIMENSIONAL STRUCTURE; CATALYTIC SPECIFICITY; MOLECULAR-DYNAMICS; ESCHERICHIA-COLI; GENE-CLUSTER; SPECTROSCOPY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
58
Recensione:
Indirizzi per estratti:
Citazione:
M.P. Crump et al., "SOLUTION STRUCTURE OF THE ACTINORHODIN POLYKETIDE SYNTHASE ACYL CARRIER PROTEIN FROM STREPTOMYCES-COELICOLOR A3(2)", Biochemistry, 36(20), 1997, pp. 6000-6008

Abstract

The solution structure of the actinorhodin acyl carrier protein ( netapo-ACP) from the polyketide synthase (PKS) of Streptomyces coelicolor A3(2) has been determined using H-1 NMR spectroscopy, representing the first polyketide synthase component for which detailed structural information has been obtained. Twenty-four structures were generated bysimulated annealing, employing 699 distance restraints and 94 dihedral angle restraints. The structure is composed, principally, of three major helices (1, 2, and 4), a shorter helix (3) and a large loon region separating helices 1 and 2. The structure is well-defined, except for a portion of the loop region (residues 18-29), the N-terminus (1-4),and a short stretch (57-61) in the loop connecting helices 2 and 3. The RMS distribution of the 24 structures about the average structure is 1.47 Angstrom for backbone atoms, 1.84 Angstrom for all heavy atoms (residues 5-86), and 1.01 Angstrom for backbone atoms over the helicalregions (5-18, 41-86). The tertiary fold of act apo-ACP shows a strong structural homology with Escherichia coli fatty acid synthase (FAS) ACP, though some structural differences exist. First, there is no evidence that act apo-ACP is conformationally averaged between two or morestates as observed in E. coli FAS ACP. Second, act apo-ACP shows a disordered N-terminus (residues 1-4) and a longer flexible loop (19-41 with 19-29 disordered) as opposed to E. coli FAS ACP where the N-terminal helix starts at residue 3 and the loop region is three amino acids shorter (16-35). Most importantly, however, although the act apo-ACP structure contains a hydrophobic core, there are in addition a number of buried hydrophilic groups, principally Arg72 and Asn79, both of which are 100% conserved in the PKS ACPs and not the FAS ACPs and may therefore play a role in stabilizing the growing polyketide chain. The structure-function relationship of act ACP is discussed in the light of these structural data and recent genetic advances in the field.

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Documento generato il 15/07/20 alle ore 13:45:59