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2fh9

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Revision as of 07:38, 18 October 2017

Structure and dimerization of the kinase domain from yeast Snf1

Structural highlights

2fh9 is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	SNF1, CAT1, CCR1, GLC2, PAS14 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SNF1_YEAST] Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The Snf1/AMPK kinases are intracellular energy sensors, and the AMPK pathway has been implicated in a variety of metabolic human disorders. Here we report the crystal structure of the kinase domain from yeast Snf1, revealing a bilobe kinase fold with greatest homology to cyclin-dependant kinase-2. Unexpectedly, the crystal structure also reveals a novel homodimer that we show also forms in solution, as demonstrated by equilibrium sedimentation, and in yeast cells, as shown by coimmunoprecipitation of differentially tagged intact Snf1. A mapping of sequence conservation suggests that dimer formation is a conserved feature of the Snf1/AMPK kinases. The conformation of the conserved alphaC helix, and the burial of the activation segment and substrate binding site within the dimer, suggests that it represents an inactive form of the kinase. Taken together, these studies suggest another layer of kinase regulation within the Snf1/AMPK family, and an avenue for development of AMPK-specific activating compounds.

Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family.,Nayak V, Zhao K, Wyce A, Schwartz MF, Lo WS, Berger SL, Marmorstein R Structure. 2006 Mar;14(3):477-85. PMID:16531232^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lo WS, Gamache ER, Henry KW, Yang D, Pillus L, Berger SL. Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms. EMBO J. 2005 Mar 9;24(5):997-1008. Epub 2005 Feb 17. PMID:15719021 doi:7600577
↑ Nayak V, Zhao K, Wyce A, Schwartz MF, Lo WS, Berger SL, Marmorstein R. Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family. Structure. 2006 Mar;14(3):477-85. PMID:16531232 doi:10.1016/j.str.2005.12.008

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fh9"

@@ Line 1: / Line 1: @@
 ==Structure and dimerization of the kinase domain from yeast Snf1==
 <StructureSection load='2fh9' size='340' side='right' caption='[[2fh9]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2fh9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FH9 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SNF1, CAT1, CCR1, GLC2, PAS14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh9 OCA], [http://pdbe.org/2fh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fh9 RCSB], [http://www.ebi.ac.uk/pdbsum/2fh9 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh9 OCA], [http://pdbe.org/2fh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fh9 RCSB], [http://www.ebi.ac.uk/pdbsum/2fh9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fh9 ProSAT]</span></td></tr>
 </table>
 == Function ==

2fh9

From Proteopedia

Revision as of 07:38, 18 October 2017

Structure and dimerization of the kinase domain from yeast Snf1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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