Structure of mouse ADP-ribosylhydrolase 3 (mARH3).
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Structure of mouse ADP-ribosylhydrolase 3 (mARH3). / Mueller-Dieckmann, Christoph; Kernstock, Stefan; Mueller-Dieckmann, Jochen; Weiss, Manfred S; Koch Nolte, Friedrich.
in: ACTA CRYSTALLOGR F, Jahrgang 64, Nr. 3, 3, 2008, S. 156-162.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Structure of mouse ADP-ribosylhydrolase 3 (mARH3).
AU - Mueller-Dieckmann, Christoph
AU - Kernstock, Stefan
AU - Mueller-Dieckmann, Jochen
AU - Weiss, Manfred S
AU - Koch Nolte, Friedrich
PY - 2008
Y1 - 2008
N2 - ADP-ribosylation is a reversible and covalent post-translational modification in which the attachment of ADP-ribose is catalyzed by ADP-ribosyltransferases and the removal of ADP-ribose is catalyzed by ADP-ribosylhydrolases. ADP-ribosylhydrolase 3 from mouse, consisting of 347 amino-acid residues, has been cloned, purified and crystallized. The three-dimensional structure has been resolved at a resolution of 1.8 A. The structure constitutes a compact all-alpha-helical protein with two Mg(2+) ions located in the active-site crevice. A structural comparison of mouse ADP-ribosylhydrolase 3 with its human orthologue shows a high degree of structural similarity. Furthermore, four prokaryotic proteins deposited in the PDB could be identified as being structurally related.
AB - ADP-ribosylation is a reversible and covalent post-translational modification in which the attachment of ADP-ribose is catalyzed by ADP-ribosyltransferases and the removal of ADP-ribose is catalyzed by ADP-ribosylhydrolases. ADP-ribosylhydrolase 3 from mouse, consisting of 347 amino-acid residues, has been cloned, purified and crystallized. The three-dimensional structure has been resolved at a resolution of 1.8 A. The structure constitutes a compact all-alpha-helical protein with two Mg(2+) ions located in the active-site crevice. A structural comparison of mouse ADP-ribosylhydrolase 3 with its human orthologue shows a high degree of structural similarity. Furthermore, four prokaryotic proteins deposited in the PDB could be identified as being structurally related.
M3 - SCORING: Zeitschriftenaufsatz
VL - 64
SP - 156
EP - 162
JO - ACTA CRYSTALLOGR F
JF - ACTA CRYSTALLOGR F
SN - 2053-230X
IS - 3
M1 - 3
ER -