1ib1
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1ib1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ib1, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF...)
Next diff →
Revision as of 15:21, 12 November 2007
|
CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX
Overview
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 Structure
1IB1 is a Protein complex structure of sequences from Homo sapiens and Ovis aries with COT as ligand. Active as Aralkylamine N-acetyltransferase, with EC number 2.3.1.87 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 17:28:23 2007
