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PDBsum entry 1v4a
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of the n-Terminal domain of escherichia coli glutamine synthetase adenylyltransferase.
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Authors
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Y.Xu,
R.Zhang,
A.Joachimiak,
P.D.Carr,
T.Huber,
S.G.Vasudevan,
D.L.Ollis.
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Ref.
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Structure, 2004,
12,
861-869.
[DOI no: ]
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PubMed id
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Abstract
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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 beta,
and polyadenylate polymerase. AT-N440 has a cluster of metal binding residues
that are conserved in polbeta-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.
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Figure 4.
Figure 4. Ribbon Diagram of Overlay Domain 3 and KNTThe
beginning and last residues of the domain 3 were labeled:
AT-N440, cyan; KNT, orange.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
861-869)
copyright 2004.
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