1ib1
CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX
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| , resolution 2.7Å | |||||||
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| Ligands: | |||||||
| Gene: | YWHAZ (Homo sapiens), AANAT OR SNAT (Ovis aries) | ||||||
| Activity: | Aralkylamine N-acetyltransferase, with EC number 2.3.1.87 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1IB1 is a Protein complex structure of sequences from Homo sapiens and Ovis aries. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation., Obsil T, Ghirlando R, Klein DC, Ganguly S, Dyda F, Cell. 2001 Apr 20;105(2):257-67. PMID:11336675
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