2nye
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2nye]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NYE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NYE FirstGlance]. <br> | <table><tr><td colspan='2'>[[2nye]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NYE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NYE FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nyc|2nyc]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nyc|2nyc]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SNF4, CAT3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SNF4, CAT3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nye OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nye RCSB], [http://www.ebi.ac.uk/pdbsum/2nye 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=2nye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nye OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nye RCSB], [http://www.ebi.ac.uk/pdbsum/2nye PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SNF4_YEAST SNF4_YEAST]] Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.<ref>PMID:7050076</ref> <ref>PMID:6392017</ref> <ref>PMID:3939253</ref> <ref>PMID:3049551</ref> <ref>PMID:2557546</ref> <ref>PMID:2169717</ref> <ref>PMID:1468623</ref> <ref>PMID:8224185</ref> <ref>PMID:8544831</ref> <ref>PMID:8985180</ref> <ref>PMID:10099331</ref> <ref>PMID:9600950</ref> <ref>PMID:10224244</ref> <ref>PMID:11486005</ref> <ref>PMID:12393914</ref> <ref>PMID:12960168</ref> <ref>PMID:18474591</ref> <ref>PMID:22019086</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 31: | Line 33: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Amodeo, G A | + | [[Category: Amodeo, G A]] |
| - | [[Category: Carlson, M | + | [[Category: Carlson, M]] |
| - | [[Category: Hong, S | + | [[Category: Hong, S]] |
| - | [[Category: Iram, S | + | [[Category: Iram, S]] |
| - | [[Category: Pirino, G | + | [[Category: Pirino, G]] |
| - | [[Category: Rudolph, M J | + | [[Category: Rudolph, M J]] |
| - | [[Category: Tong, L | + | [[Category: Tong, L]] |
[[Category: Amp kinase]] | [[Category: Amp kinase]] | ||
[[Category: Bateman2 domain]] | [[Category: Bateman2 domain]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Snf4]] | [[Category: Snf4]] | ||
Revision as of 19:35, 24 December 2014
Crystal structure of the Bateman2 domain of yeast Snf4
| |||||||||||
