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PDBsum entry 1ib1
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Signaling protein/transferase
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PDB id
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1ib1
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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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Crystal structure of the 14-3-3zeta:serotonin n-Acetyltransferase complex. A role for scaffolding in enzyme regulation.
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Authors
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T.Obsil,
R.Ghirlando,
D.C.Klein,
S.Ganguly,
F.Dyda.
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Ref.
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Cell, 2001,
105,
257-267.
[DOI no: ]
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PubMed id
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Abstract
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Serotonin N-acetyltransferase (AANAT) controls the daily rhythm in melatonin
synthesis. When isolated from tissue, AANAT copurifies with isoforms epsilon and
zeta of 14-3-3. We have determined the structure of AANAT bound to 14-3-3zeta,
an association that is phosphorylation dependent. AANAT is bound in the central
channel of the 14-3-3zeta dimer, and is held in place by extensive interactions
both with the amphipathic phosphopeptide binding groove of 14-3-3zeta and with
other parts of the central channel. Thermodynamic and activity measurements,
together with crystallographic analysis, indicate that binding of AANAT by
14-3-3zeta modulates AANAT's activity and affinity for its substrates by
stabilizing a region of AANAT involved in substrate binding.
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Figure 1.
Figure 1. Structure of the 14-3-3ζ:pAANAT[1–201] Complex
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Figure 2.
Figure 2. Interaction Between pAANAT[1–201] and a Monomer
of 14-3-3ζ
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2001,
105,
257-267)
copyright 2001.
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