1ib1: Difference between revisions

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New page: left|200px<br /> <applet load="1ib1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ib1, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1ib1.gif|left|200px]]<br />
[[Image:1ib1.gif|left|200px]]<br /><applet load="1ib1" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1ib1" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1ib1, resolution 2.7&Aring;" />
caption="1ib1, resolution 2.7&Aring;" />
'''CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX'''<br />
'''CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX'''<br />


==Overview==
==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.
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==
==About this Structure==
1IB1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] with COT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aralkylamine_N-acetyltransferase Aralkylamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.87 2.3.1.87] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IB1 OCA].  
1IB1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] with <scene name='pdbligand=COT:'>COT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aralkylamine_N-acetyltransferase Aralkylamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.87 2.3.1.87] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IB1 OCA].  


==Reference==
==Reference==
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[[Category: Ganguly, S.]]
[[Category: Ganguly, S.]]
[[Category: Ghirlando, R.]]
[[Category: Ghirlando, R.]]
[[Category: Klein, D.C.]]
[[Category: Klein, D C.]]
[[Category: Obsil, T.]]
[[Category: Obsil, T.]]
[[Category: COT]]
[[Category: COT]]
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[[Category: signal transduction]]
[[Category: signal transduction]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:28:23 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:55 2008''

Revision as of 14:09, 21 February 2008

File:1ib1.gif


1ib1, resolution 2.7Å

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CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX

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 with as ligand. Active as Aralkylamine N-acetyltransferase, with EC number 2.3.1.87 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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