TY - JOUR
T1 - Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase
AU - Xu, Yibin
AU - Zhang, Rongguand
AU - Joachimiak, Andrzej
AU - Carr, Paul D.
AU - Huber, Thomas
AU - Vasudevan, Subhash G.
AU - Ollis, David L.
PY - 2004/5
Y1 - 2004/5
N2 - We report the crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase that catalyzes the reversible nucleotidylation of glutamine synthetase (GS), a key enzyme in nitrogen assimilation. This domain (AT-N440) catalyzes the deadenylylation and subsequent activation of GS. The structure has been divided into three subdomains, two of which bear some similarity to kanamycin nucleotidyltransferase (KNT). However, the orientation of the two domains in AT-N440 differs from that in KNT. The active site of AT-N440 has been identified on the basis of structural comparisons with KNT, DNA polymerase β, and polyadenylate polymerase. AT-N440 has a cluster of metal binding residues that are conserved in polβ-like nucleotidyl transferases. The location of residues conserved in all ATase sequences was found to cluster around the active site. Many of these residues are very likely to play a role in catalysis, substrate binding, or effector binding.
AB - We report the crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase that catalyzes the reversible nucleotidylation of glutamine synthetase (GS), a key enzyme in nitrogen assimilation. This domain (AT-N440) catalyzes the deadenylylation and subsequent activation of GS. The structure has been divided into three subdomains, two of which bear some similarity to kanamycin nucleotidyltransferase (KNT). However, the orientation of the two domains in AT-N440 differs from that in KNT. The active site of AT-N440 has been identified on the basis of structural comparisons with KNT, DNA polymerase β, and polyadenylate polymerase. AT-N440 has a cluster of metal binding residues that are conserved in polβ-like nucleotidyl transferases. The location of residues conserved in all ATase sequences was found to cluster around the active site. Many of these residues are very likely to play a role in catalysis, substrate binding, or effector binding.
UR - http://www.scopus.com/inward/record.url?scp=2342628394&partnerID=8YFLogxK
U2 - 10.1016/j.str.2004.02.029
DO - 10.1016/j.str.2004.02.029
M3 - Article
SN - 0969-2126
VL - 12
SP - 861
EP - 869
JO - Structure
JF - Structure
IS - 5
ER -