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.


2pnr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pnr.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2pnr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pnr| PDB=2pnr | SCENE= }}
{{STRUCTURE_2pnr| PDB=2pnr | SCENE= }}
-
'''Crystal Structure of the asymmetric Pdk3-l2 Complex'''
+
===Crystal Structure of the asymmetric Pdk3-l2 Complex===
-
==Overview==
+
<!--
-
A homodimer of pyruvate dehydrogenase kinase (PDHK) is an integral part of pyruvate dehydrogenase complex (PDC) to which it is anchored primarily through the inner lipoyl-bearing domains (L2) of transacetylase component. The catalytic cycle of PDHK and its translocation over the PDC surface is thought to be mediated by the "symmetric" and "asymmetric" modes, in which the PDHK dimer binds to two and one L2-domain(s), respectively. Whereas the structure of the symmetric PDHK/L2 complex was reported, the structural organization and functional role of the asymmetric complex remain obscure. Here, we report the crystal structure of the asymmetric PDHK3/L2 complex that reveals several functionally important features absent from the previous structures. First, the PDHK3 subunits have distinct conformations: one subunit exhibits "open" and the other "closed" configuration of the putative substrate-binding cleft. Second, access to the closed cleft is additionally restricted by local unwinding of the adjacent alpha-helix. Modeling indicates that the target peptide might gain access to the PDHK active center through the open but not through the closed cleft. Third, the ATP-binding loop in one PDHK3 subunit adopts an open conformation, implying that the nucleotide loading into the active site is mediated by the inactive "pre-insertion" binding mode. Altogether our data suggest that the asymmetric complex represents a physiological state in which binding of a single L2-domain activates one of the PDHK protomers while inactivating another. Thus, the L2-domains likely act not only as the structural anchors but also modulate the catalytic cycle of PDHK.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17532006}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17532006 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17532006}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Pyruvate dehydrogenase kinase 3]]
[[Category: Pyruvate dehydrogenase kinase 3]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:29:52 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:22:26 2008''

Revision as of 01:22, 28 July 2008

Image:2pnr.png

Template:STRUCTURE 2pnr

Crystal Structure of the asymmetric Pdk3-l2 Complex

Template:ABSTRACT PUBMED 17532006

About this Structure

2PNR is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications., Devedjiev Y, Steussy CN, Vassylyev DG, J Mol Biol. 2007 Jul 13;370(3):407-16. Epub 2007 May 10. PMID:17532006

Page seeded by OCA on Mon Jul 28 04:22:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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