2dyt: Difference between revisions

Revision as of 10:22, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2dyt.png

Template:STRUCTURE 2dyt

The crystal structure of Saccharomyces cerevisiae Atg3The crystal structure of Saccharomyces cerevisiae Atg3

Template:ABSTRACT PUBMED 17227760

About this StructureAbout this Structure

2DYT is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation., Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F, J Biol Chem. 2007 Mar 16;282(11):8036-43. Epub 2007 Jan 16. PMID:17227760

Crystallization and preliminary X-ray analysis of Atg3., Yamada Y, Suzuki NN, Fujioka Y, Ichimura Y, Ohsumi Y, Inagaki F, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):1016-7. Epub 2006 Sep 30. PMID:17012800

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2dyt.gif|left|200px]]
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 {{STRUCTURE_2dyt|  PDB=2dyt  |  SCENE=  }}
-'''The crystal structure of Saccharomyces cerevisiae Atg3'''
+===The crystal structure of Saccharomyces cerevisiae Atg3===
-==Overview==
+<!--
-Atg3 is an E2-like enzyme that catalyzes the conjugation of Atg8 and phosphatidylethanolamine (PE). The Atg8-PE conjugate is essential for autophagy, which is the bulk degradation process of cytoplasmic components by the vacuolar/lysosomal system. We report here the crystal structure of Saccharomyces cerevisiae Atg3 at 2.5-A resolution. Atg3 has an alpha/beta-fold, and its core region is topologically similar to canonical E2 enzymes. Atg3 has two regions inserted in the core region, one of which consists of approximately 80 residues and has a random coil structure in solution and another with a long alpha-helical structure that protrudes from the core region as far as 30 A. In vivo and in vitro analyses suggested that the former region is responsible for binding Atg7, an E1-like enzyme, and that the latter is responsible for binding Atg8. A sulfate ion was bound near the catalytic cysteine of Atg3, suggesting a possible binding site for the phosphate moiety of PE. The structure of Atg3 provides a molecular basis for understanding the unique lipidation reaction that Atg3 carries out.
+The line below this paragraph, {{ABSTRACT_PUBMED_17227760}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17227760 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17227760}}
 ==About this Structure==
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 ==Reference==
 The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation., Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F, J Biol Chem. 2007 Mar 16;282(11):8036-43. Epub 2007 Jan 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17227760 17227760]
+Crystallization and preliminary X-ray analysis of Atg3., Yamada Y, Suzuki NN, Fujioka Y, Ichimura Y, Ohsumi Y, Inagaki F, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):1016-7. Epub 2006 Sep 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17012800 17012800]
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
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 [[Category: E2 fold]]
 [[Category: Ligase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 01:38:08 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:22:41 2008''