Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus
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Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus. / Lauritsen, Iben H.; Willemoës, Martin; Jensen, Kaj Frank; Johansson, Eva; Harris, Pernille.
I: Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, Bind 67, Nr. 2, 2011, s. 201-208.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus
AU - Lauritsen, Iben H.
AU - Willemoës, Martin
AU - Jensen, Kaj Frank
AU - Johansson, Eva
AU - Harris, Pernille
PY - 2011
Y1 - 2011
N2 - CTP synthase catalyzes the last committed step in de novo pyrimidinenucleotidebiosynthesis. Active CTP synthase is a tetrameric enzyme composedof a dimer of dimers. The tetramer is favoured in the presence of the substratenucleotides ATP and UTP; when saturated with nucleotide, the tetramercompletely dominates the oligomeric state of the enzyme. Furthermore,phosphorylation has been shown to regulate the oligomeric states of theenzymes from yeast and human. The crystal structure of a dimeric form of CTPsynthase from Sulfolobus solfataricus has been determined at 2.5 A ° resolution.A comparison of the dimeric interface with the intermolecular interfaces in thetetrameric structures of Thermus thermophilus CTP synthase and Escherichiacoli CTP synthase shows that the dimeric interfaces are almost identical in thethree systems. Residues that are involved in the tetramerization of S. solfataricusCTP synthase according to a structural alignment with the E. coli enzyme allhave large thermal parameters in the dimeric form. Furthermore, they are seento undergo substantial movement upon tetramerization.
AB - CTP synthase catalyzes the last committed step in de novo pyrimidinenucleotidebiosynthesis. Active CTP synthase is a tetrameric enzyme composedof a dimer of dimers. The tetramer is favoured in the presence of the substratenucleotides ATP and UTP; when saturated with nucleotide, the tetramercompletely dominates the oligomeric state of the enzyme. Furthermore,phosphorylation has been shown to regulate the oligomeric states of theenzymes from yeast and human. The crystal structure of a dimeric form of CTPsynthase from Sulfolobus solfataricus has been determined at 2.5 A ° resolution.A comparison of the dimeric interface with the intermolecular interfaces in thetetrameric structures of Thermus thermophilus CTP synthase and Escherichiacoli CTP synthase shows that the dimeric interfaces are almost identical in thethree systems. Residues that are involved in the tetramerization of S. solfataricusCTP synthase according to a structural alignment with the E. coli enzyme allhave large thermal parameters in the dimeric form. Furthermore, they are seento undergo substantial movement upon tetramerization.
KW - Faculty of Science
KW - CTP synthase
KW - dimer-tetramer equilibrium
KW - nucleotide metabolism
U2 - 10.1107/S1744309110052334
DO - 10.1107/S1744309110052334
M3 - Journal article
C2 - 21301086
VL - 67
SP - 201
EP - 208
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
SN - 2053-230X
IS - 2
ER -
ID: 32670780