First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.

2vk1

From Proteopedia

Jump to: navigation, search


2vk1, resolution 1.71Å ()
Ligands: , ,
Activity: Pyruvate decarboxylase, with EC number 4.1.1.1
Related: 1qpb, 1pyd, 1pvd
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE PYRUVATE DECARBOXYLASE VARIANT D28A IN COMPLEX WITH ITS SUBSTRATE

Publication Abstract from PubMed

The mechanism by which the enzyme pyruvate decarboxylase from two yeast species is activated allosterically has been elucidated. A total of seven three-dimensional structures of the enzyme, of enzyme variants, or of enzyme complexes from two yeast species, three of them reported here for the first time, provide detailed atomic resolution snapshots along the activation coordinate. The prime event is the covalent binding of the substrate pyruvate to the side chain of cysteine 221, thus forming a thiohemiketal. This reaction causes the shift of a neighboring amino acid, which eventually leads to the rigidification of two otherwise flexible loops, one of which provides two histidine residues necessary to complete the enzymatically competent active site architecture. The structural data are complemented and supported by kinetic investigations and binding studies, providing a consistent picture of the structural changes occurring upon enzyme activation.

Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation., Kutter S, Weiss MS, Wille G, Golbik R, Spinka M, Konig S, J Biol Chem. 2009 May 1;284(18):12136-44. Epub 2009 Feb 26. PMID:19246454

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2vk1 is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

See Also

Reference

  • Kutter S, Weiss MS, Wille G, Golbik R, Spinka M, Konig S. Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation. J Biol Chem. 2009 May 1;284(18):12136-44. Epub 2009 Feb 26. PMID:19246454 doi:10.1074/jbc.M806228200

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools