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Titolo:
PREDICTING THE STRUCTURE OF THE LIGHT-HARVESTING COMPLEX-II OF RHODOSPIRILLUM-MOLISCHIANUM
Autore:
HU XC; XU D; HAMER K; SCHULTEN K; KOEPKE J; MICHEL H;
Indirizzi:
UNIV ILLINOIS,BECKMAN INST,405 N MATHEWS AVE URBANA IL 61801 UNIV ILLINOIS,BECKMAN INST URBANA IL 61801 MAX PLANCK INST BIOCHEM,MOLEK MEMBRANBIOL ABT W-6000 FRANKFURT GERMANY
Titolo Testata:
Protein science
fascicolo: 9, volume: 4, anno: 1995,
pagine: 1670 - 1682
SICI:
0961-8368(1995)4:9<1670:PTSOTL>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOTOSYNTHETIC REACTION CENTER; PROTEIN-STRUCTURE PREDICTION; AMINO-ACID-SEQUENCES; MEMBRANE-PROTEINS; RHODOPSEUDOMONAS-VIRIDIS; SECONDARY STRUCTURE; ANTENNA COMPLEXES; B800-850; POLYPEPTIDES; SPHAEROIDES;
Keywords:
INTEGRAL MEMBRANE PROTEIN; LIGHT-HARVESTING COMPLEX; MOLECULAR REPLACEMENT; PROTEIN FOLDING; PROTEIN STRUCTURE; PURPLE BACTERIA; SEQUENCE ANALYSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
63
Recensione:
Indirizzi per estratti:
Citazione:
X.C. Hu et al., "PREDICTING THE STRUCTURE OF THE LIGHT-HARVESTING COMPLEX-II OF RHODOSPIRILLUM-MOLISCHIANUM", Protein science, 4(9), 1995, pp. 1670-1682

Abstract

We attempted to predict through computer modeling the structure of the light-harvesting complex II (LH-II) of Rhodospirillum molischianum, before the impending publication of the structure of a homologous protein solved by means of X-ray diffraction. The protein studied is an integral membrane protein of 16 independent polypeptides, 8 alpha-apoproteins and 8 beta-apoproteins, which aggregate and bind to 24 bacteriochlorophyll-a's and 12 lycopenes. Available diffraction data of a crystal of the protein, which could not be phased due to a lack of heavy metal derivatives, served to test the predicted structure, guiding the search. In order to determine the secondary structure, hydropathy analysis was performed to identify the putative transmembrane segments and multiple sequence alignment propensity analyses were used to pinpoint the exact sites of the 20-residue-long transmembrane segment and the 4-residue-long terminal sequence at both ends, which were independentlyverified and improved by homology modeling. A consensus assignment for the secondary structure was derived from a combination of all the prediction methods used. Three-dimensional structures for the alpha- andthe beta-apoprotein were built by comparative modeling. The resultingtertiary structures are combined, using X-PLOR, into an alpha beta dimer pair with bacteriochlorophyll-a's attached under constraints provided by site-directed mutagenesis and spectral data. The alpha beta dimer pairs were then aggregated into a quaternary structure through further molecular dynamics simulations and energy minimization. The structure of LH-II so determined is an octamer of alpha beta heterodimers forming a ring with a diameter of 70 Angstrom.

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Documento generato il 24/11/20 alle ore 14:18:25