2QQC

E109Q mutant of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii

Summary for 2QQC

• Entry DOI: 10.2210/pdb2qqc/pdb
• Related: 2QQD
• Descriptor: Pyruvoyl-dependent arginine decarboxylase subunit beta, Pyruvoyl-dependent arginine decarboxylase subunit alpha, AGMATINE, ... (5 entities in total)
• Functional Keywords: arginine decarboxylase, pyruvoyl, decarboxylation, autoprocessing, serinolysis, lyase, pyruvate
• Biological source: Methanocaldococcus jannaschii; More
• Total number of polymer chains: 12
• Total formula weight: 108430.01

Authors

Ealick, S.E.,Soriano, E.S. (deposition date: 2007-07-26, release date: 2008-03-18, Last modification date: 2024-10-16)

Primary citation

Soriano, E.V.,McCloskey, D.E.,Kinsland, C.,Pegg, A.E.,Ealick, S.E.
Structures of the N47A and E109Q mutant proteins of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii.
Acta Crystallogr.,Sect.D, 64:377-382, 2008

PubMed Abstract: Pyruvoyl-dependent arginine decarboxylase (PvlArgDC) catalyzes the first step of the polyamine-biosynthetic pathway in plants and some archaebacteria. The pyruvoyl group of PvlArgDC is generated by an internal autoserinolysis reaction at an absolutely conserved serine residue in the proenzyme, resulting in two polypeptide chains. Based on the native structure of PvlArgDC from Methanococcus jannaschii, the conserved residues Asn47 and Glu109 were proposed to be involved in the decarboxylation and autoprocessing reactions. N47A and E109Q mutant proteins were prepared and the three-dimensional structure of each protein was determined at 2.0 A resolution. The N47A and E109Q mutant proteins showed reduced decarboxylation activity compared with the wild-type PvlArgDC. These residues may also be important for the autoprocessing reaction, which utilizes a mechanism similar to that of the decarboxylation reaction.

PubMed: 18391404
DOI: 10.1107/S0907444908000474

Experimental method

X-RAY DIFFRACTION (2 Å)