2p9t: Difference between revisions

Revision as of 09:32, 29 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:2p9t.png

Template:STRUCTURE 2p9t

Crystal Structure of Phosphoglycerate Kinase-2 bound to 3-phosphoglycerateCrystal Structure of Phosphoglycerate Kinase-2 bound to 3-phosphoglycerate

Template:ABSTRACT PUBMED 18004764

About this StructureAbout this Structure

2P9T is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

X-ray analysis of phosphoglycerate kinase 2, a sperm-specific isoform from Mus musculus., Sawyer GM, Monzingo AF, Poteet EC, O'Brien DA, Robertus JD, Proteins. 2007 Nov 14;. PMID:18004764

Page seeded by OCA on Tue Jul 29 09:32:03 2008

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

OCA

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 {{STRUCTURE_2p9t|  PDB=2p9t  |  SCENE=  }}
-'''Crystal Structure of Phosphoglycerate Kinase-2 bound to 3-phosphoglycerate'''
+===Crystal Structure of Phosphoglycerate Kinase-2 bound to 3-phosphoglycerate===
-==Overview==
+<!--
-Phosphoglycerate kinase 2 (PGK2) is an isozyme of the glycolytic pathway that provides ATP required for sperm motility. It is encoded by an autosomal retrogene that is expressed only during spermatogenesis, concomitant with the inactivation of the X-linked Pgk1 gene. PGK2 from the mouse, Mus musculus, has been overexpressed from a plasmid in bacteria and purified. It was crystallized in three forms: as the apoenzyme, as a complex with 3-phosphoglycerate (3PG), and as a complex with 3PG and ATP. The crystal structures were solved to 2.7, 2.0, and 2.7 A resolutions, respectively. The overall fold is nearly identical with previously solved mammalian PGK1 molecules. The apoenzyme is in the "open" form; that is the N-terminal domain that can bind 3PG and the C-terminal domain that binds ATP are too far apart for the substrates to interact. Binding 3PG causes a 13 degrees rotation that partially closes the structure and causes helix 13, which is disordered in the unliganded structure, to stabilize. Binding ATP leaves the protein in the open configuration but also causes helix 13 to be ordered. Sequence alignment suggests that the active site of PGK2 is essentially identical to that of the cytoplasmic PGK1, but significant differences accumulate on a side of the C-terminal domain away from the active site. These changes may mediate the binding of this isoform to other proteins within the sperm flagellum, while still allowing the hinging action between the domains that is essential to catalytic activity. Proteins 2007. (c) 2007 Wiley-Liss, Inc.
+The line below this paragraph, {{ABSTRACT_PUBMED_18004764}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18004764 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18004764}}
 ==About this Structure==
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 [[Category: Phosphoglycerate kinse]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:26:48 2008''
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