This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2li5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2li5.png|left|200px]]
+
==NMR structure of Atg8-Atg7C30 complex==
 +
<StructureSection load='2li5' size='340' side='right' caption='[[2li5]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>
 +
== Structural highlights ==
 +
[[2li5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LI5 OCA]. <br>
 +
<b>Related:</b> [[2kwc|2kwc]]<br>
 +
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
 +
== Publication Abstract from PubMed ==
 +
E1 enzymes activate ubiquitin-like proteins and transfer them to cognate E2 enzymes. Atg7, a noncanonical E1, activates two ubiquitin-like proteins, Atg8 and Atg12, and plays a crucial role in autophagy. Here, we report crystal structures of full-length Atg7 and its C-terminal domain bound to Atg8 and MgATP, as well as a solution structure of Atg8 bound to the extreme C-terminal domain (ECTD) of Atg7. The unique N-terminal domain (NTD) of Atg7 is responsible for Atg3 (E2) binding, whereas its C-terminal domain is comprised of a homodimeric adenylation domain (AD) and ECTD. The structural and biochemical data demonstrate that Atg8 is initially recognized by the C-terminal tail of ECTD and is then transferred to an AD, where the Atg8 C terminus is attacked by the catalytic cysteine to form a thioester bond. Atg8 is then transferred via a trans mechanism to the Atg3 bound to the NTD of the opposite protomer within a dimer.
-
<!--
+
Structural basis of Atg8 activation by a homodimeric E1, Atg7.,Noda NN, Satoo K, Fujioka Y, Kumeta H, Ogura K, Nakatogawa H, Ohsumi Y, Inagaki F Mol Cell. 2011 Nov 4;44(3):462-75. PMID:22055191<ref>PMID:22055191</ref>
-
The line below this paragraph, containing "STRUCTURE_2li5", creates the "Structure Box" on the page.
+
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
-
or leave the SCENE parameter empty for the default display.
+
-
-->
+
-
{{STRUCTURE_2li5| PDB=2li5 | SCENE= }}
+
-
===NMR structure of Atg8-Atg7C30 complex===
+
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-
 
+
== References ==
-
 
+
<references/>
-
<!--
+
__TOC__
-
The line below this paragraph, {{ABSTRACT_PUBMED_22055191}}, adds the Publication Abstract to the page
+
</StructureSection>
-
(as it appears on PubMed at http://www.pubmed.gov), where 22055191 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_22055191}}
+
-
 
+
-
==About this Structure==
+
-
[[2li5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LI5 OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:022055191</ref><references group="xtra"/>
+
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Fujioka, Y.]]
[[Category: Fujioka, Y.]]

Revision as of 08:37, 30 April 2014

NMR structure of Atg8-Atg7C30 complex

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2li5"
Personal tools