1z0m
From Proteopedia
(New page: 200px<br /><applet load="1z0m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z0m, resolution 1.910Å" /> '''the glycogen-bindin...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1z0m.gif|left|200px]]<br /><applet load="1z0m" size=" | + | [[Image:1z0m.gif|left|200px]]<br /><applet load="1z0m" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z0m, resolution 1.910Å" /> | caption="1z0m, resolution 1.910Å" /> | ||
'''the glycogen-binding domain of the AMP-activated protein kinase beta1 subunit'''<br /> | '''the glycogen-binding domain of the AMP-activated protein kinase beta1 subunit'''<br /> | ||
==Overview== | ==Overview== | ||
| - | AMP-activated protein kinase (AMPK) coordinates cellular metabolism in | + | AMP-activated protein kinase (AMPK) coordinates cellular metabolism in response to energy demand as well as to a variety of stimuli. The AMPK beta subunit acts as a scaffold for the alpha catalytic and gamma regulatory subunits and targets the AMPK heterotrimer to glycogen. We have determined the structure of the AMPK beta glycogen binding domain in complex with beta-cyclodextrin. The structure reveals a carbohydrate binding pocket that consolidates all known aspects of carbohydrate binding observed in starch binding domains into one site, with extensive contact between several residues and five glucose units. beta-cyclodextrin is held in a pincer-like grasp with two tryptophan residues cradling two beta-cyclodextrin glucose units and a leucine residue piercing the beta-cyclodextrin ring. Mutation of key beta-cyclodextrin binding residues either partially or completely prevents the glycogen binding domain from binding glycogen. Modeling suggests that this binding pocket enables AMPK to interact with glycogen anywhere across the carbohydrate's helical surface. |
==About this Structure== | ==About this Structure== | ||
| - | 1Z0M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with BCD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1Z0M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=BCD:'>BCD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0M OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Denderen, B | + | [[Category: Denderen, B J.van.]] |
| - | [[Category: Feil, S | + | [[Category: Feil, S C.]] |
[[Category: Gupta, A.]] | [[Category: Gupta, A.]] | ||
| - | [[Category: Kemp, B | + | [[Category: Kemp, B E.]] |
| - | [[Category: Parker, M | + | [[Category: Parker, M W.]] |
[[Category: Polekhina, G.]] | [[Category: Polekhina, G.]] | ||
[[Category: Stapleton, D.]] | [[Category: Stapleton, D.]] | ||
| Line 23: | Line 23: | ||
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:00 2008'' |
Revision as of 14:11, 21 February 2008
|
the glycogen-binding domain of the AMP-activated protein kinase beta1 subunit
Overview
AMP-activated protein kinase (AMPK) coordinates cellular metabolism in response to energy demand as well as to a variety of stimuli. The AMPK beta subunit acts as a scaffold for the alpha catalytic and gamma regulatory subunits and targets the AMPK heterotrimer to glycogen. We have determined the structure of the AMPK beta glycogen binding domain in complex with beta-cyclodextrin. The structure reveals a carbohydrate binding pocket that consolidates all known aspects of carbohydrate binding observed in starch binding domains into one site, with extensive contact between several residues and five glucose units. beta-cyclodextrin is held in a pincer-like grasp with two tryptophan residues cradling two beta-cyclodextrin glucose units and a leucine residue piercing the beta-cyclodextrin ring. Mutation of key beta-cyclodextrin binding residues either partially or completely prevents the glycogen binding domain from binding glycogen. Modeling suggests that this binding pocket enables AMPK to interact with glycogen anywhere across the carbohydrate's helical surface.
About this Structure
1Z0M is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for glycogen recognition by AMP-activated protein kinase., Polekhina G, Gupta A, van Denderen BJ, Feil SC, Kemp BE, Stapleton D, Parker MW, Structure. 2005 Oct;13(10):1453-62. PMID:16216577
Page seeded by OCA on Thu Feb 21 16:11:00 2008
