Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus

Publication: Research - peer-reviewJournal article – Annual report year: 2011

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Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus. / Lauritsen, Iben; Willemo¨es, Martin; Jensen, Kaj Frank; Johansson, Eva; Harris, Pernille.

In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, Vol. F67, No. 2, 2011, p. 201-208.

Publication: Research - peer-reviewJournal article – Annual report year: 2011

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Lauritsen, Iben; Willemo¨es, Martin; Jensen, Kaj Frank; Johansson, Eva; Harris, Pernille / Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus.

In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, Vol. F67, No. 2, 2011, p. 201-208.

Publication: Research - peer-reviewJournal article – Annual report year: 2011

Bibtex

@article{e085b2bca7484789a362bd459c71e3a3,
title = "Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus",
publisher = "Wiley-Blackwell Munksgaard",
author = "Iben Lauritsen and Martin Willemo¨es and Jensen, {Kaj Frank} and Eva Johansson and Pernille Harris",
note = "© 2011 International Union of Crystallography",
year = "2011",
doi = "10.1107/S1744309110052334",
volume = "F67",
number = "2",
pages = "201--208",
journal = "Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online",
issn = "1744-3091",

}

RIS

TY - JOUR

T1 - Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus

A1 - Lauritsen,Iben

A1 - Willemo¨es,Martin

A1 - Jensen,Kaj Frank

A1 - Johansson,Eva

A1 - Harris,Pernille

AU - Lauritsen,Iben

AU - Willemo¨es,Martin

AU - Jensen,Kaj Frank

AU - Johansson,Eva

AU - Harris,Pernille

PB - Wiley-Blackwell Munksgaard

PY - 2011

Y1 - 2011

N2 - CTP synthase catalyzes the last committed step in de novo pyrimidine-nucleotide biosynthesis. Active CTP synthase is a tetrameric enzyme composed of a dimer of dimers. The tetramer is favoured in the presence of the substrate nucleotides ATP and UTP; when saturated with nucleotide, the tetramer completely dominates the oligomeric state of the enzyme. Furthermore, phosphorylation has been shown to regulate the oligomeric states of the enzymes from yeast and human. The crystal structure of a dimeric form of CTP synthase from Sulfolobus solfataricus has been determined at 2.5 Å resolution. A comparison of the dimeric interface with the intermolecular interfaces in the tetrameric structures of Thermus thermophilus CTP synthase and Escherichia coli CTP synthase shows that the dimeric interfaces are almost identical in the three systems. Residues that are involved in the tetramerization of S. solfataricus CTP synthase according to a structural alignment with the E. coli enzyme all have large thermal parameters in the dimeric form. Furthermore, they are seen to undergo substantial movement upon tetramerization.

AB - CTP synthase catalyzes the last committed step in de novo pyrimidine-nucleotide biosynthesis. Active CTP synthase is a tetrameric enzyme composed of a dimer of dimers. The tetramer is favoured in the presence of the substrate nucleotides ATP and UTP; when saturated with nucleotide, the tetramer completely dominates the oligomeric state of the enzyme. Furthermore, phosphorylation has been shown to regulate the oligomeric states of the enzymes from yeast and human. The crystal structure of a dimeric form of CTP synthase from Sulfolobus solfataricus has been determined at 2.5 Å resolution. A comparison of the dimeric interface with the intermolecular interfaces in the tetrameric structures of Thermus thermophilus CTP synthase and Escherichia coli CTP synthase shows that the dimeric interfaces are almost identical in the three systems. Residues that are involved in the tetramerization of S. solfataricus CTP synthase according to a structural alignment with the E. coli enzyme all have large thermal parameters in the dimeric form. Furthermore, they are seen to undergo substantial movement upon tetramerization.

KW - Nucleotide metabolism

KW - Dimer-tetramer equilibrium

KW - CTP synthase

UR - http://journals.iucr.org.globalproxy.cvt.dk/f/issues/2011/02/00/sx5102/sx5102.pdf

U2 - 10.1107/S1744309110052334

DO - 10.1107/S1744309110052334

JO - Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online

JF - Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online

SN - 1744-3091

IS - 2

VL - F67

SP - 201

EP - 208

ER -