From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2pnq.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:2pnq.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2pnq| PDB=2pnq | SCENE= }} | | {{STRUCTURE_2pnq| PDB=2pnq | SCENE= }} |
| | | | |
| - | '''Crystal structure of pyruvate dehydrogenase phosphatase 1 (PDP1)'''
| + | ===Crystal structure of pyruvate dehydrogenase phosphatase 1 (PDP1)=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Pyruvate dehydrogenase phosphatase 1 (PDP1) catalyzes dephosphorylation of pyruvate dehydrogenase (E1) in the mammalian pyruvate dehydrogenase complex (PDC), whose activity is regulated by the phosphorylation-dephosphorylation cycle by the corresponding protein kinases (PDHKs) and phosphatases. The activity of PDP1 is greatly enhanced through Ca2+ -dependent binding of the catalytic subunit (PDP1c) to the L2 (inner lipoyl) domain of dihydrolipoyl acetyltransferase (E2), which is also integrated in PDC. Here, we report the crystal structure of the rat PDP1c at 1.8 A resolution. The structure reveals that PDP1 belongs to the PPM family of protein serine/threonine phosphatases, which, in spite of a low level of sequence identity, share the structural core consisting of the central beta-sandwich flanked on both sides by loops and alpha-helices. Consistent with the previous studies, two well-fixed magnesium ions are coordinated by five active site residues and five water molecules in the PDP1c catalytic center. Structural analysis indicates that, while the central portion of the PDP1c molecule is highly conserved among the members of the PPM protein family, a number of structural insertions and deletions located at the periphery of PDP1c likely define its functional specificity towards the PDC. One notable feature of PDP1c is a long insertion (residues 98-151) forming a unique hydrophobic pocket on the surface that likely accommodates the lipoyl moiety of the E2 domain in a fashion similar to that of PDHKs. The cavity, however, appears more open than in PDHK, suggesting that its closure may be required to achieve tight, specific binding of the lipoic acid. We propose a mechanism in which the closure of the lipoic acid binding site is triggered by the formation of the intermolecular (PDP1c/L2) Ca2+ binding site in a manner reminiscent of the Ca2+ -induced closure of the regulatory domain of troponin C.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17532339}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17532339 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17532339}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| | [[Category: Pdp1c]] | | [[Category: Pdp1c]] |
| | [[Category: Pyruvate dehydrogenase phosphatase 1]] | | [[Category: Pyruvate dehydrogenase phosphatase 1]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:29:44 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:27:27 2008'' |
Revision as of 21:27, 28 July 2008
Template:STRUCTURE 2pnq
Crystal structure of pyruvate dehydrogenase phosphatase 1 (PDP1)
Template:ABSTRACT PUBMED 17532339
About this Structure
2PNQ is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of pyruvate dehydrogenase phosphatase 1 and its functional implications., Vassylyev DG, Symersky J, J Mol Biol. 2007 Jul 13;370(3):417-26. Epub 2007 May 10. PMID:17532339
Page seeded by OCA on Tue Jul 29 00:27:27 2008
