3NZQ

Crystal Structure of Biosynthetic arginine decarboxylase ADC (SpeA) from Escherichia coli, Northeast Structural Genomics Consortium Target ER600

Summary for 3NZQ

• Entry DOI: 10.2210/pdb3nzq/pdb
• Descriptor: Biosynthetic arginine decarboxylase, SULFATE ION (3 entities in total)
• Functional Keywords: alpha-beta protein, structural genomics, psi-biology, protein structure initiative, northeast structural genomics consortium, nesg, lyase
• Biological source: Escherichia coli
• Cellular location: Periplasm: P21170
• Total number of polymer chains: 2
• Total formula weight: 150475.03

Authors

Forouhar, F.,Lew, S.,Seetharaman, J.,Sahdev, S.,Xiao, R.,Ciccosanti, C.,Belote, R.L.,Everett, J.K.,Nair, R.,Acton, T.B.,Rost, B.,Montelione, G.T.,Hunt, J.F.,Tong, L.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2010-07-16, release date: 2010-09-01, Last modification date: 2024-02-21)

Primary citation

Forouhar, F.,Lew, S.,Seetharaman, J.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Tong, L.
Structures of bacterial biosynthetic arginine decarboxylases.
Acta Crystallogr.,Sect.F, 66:1562-1566, 2010

PubMed Abstract: Biosynthetic arginine decarboxylase (ADC; also known as SpeA) plays an important role in the biosynthesis of polyamines from arginine in bacteria and plants. SpeA is a pyridoxal-5'-phosphate (PLP)-dependent enzyme and shares weak sequence homology with several other PLP-dependent decarboxylases. Here, the crystal structure of PLP-bound SpeA from Campylobacter jejuni is reported at 3.0 Å resolution and that of Escherichia coli SpeA in complex with a sulfate ion is reported at 3.1 Å resolution. The structure of the SpeA monomer contains two large domains, an N-terminal TIM-barrel domain followed by a β-sandwich domain, as well as two smaller helical domains. The TIM-barrel and β-sandwich domains share structural homology with several other PLP-dependent decarboxylases, even though the sequence conservation among these enzymes is less than 25%. A similar tetramer is observed for both C. jejuni and E. coli SpeA, composed of two dimers of tightly associated monomers. The active site of SpeA is located at the interface of this dimer and is formed by residues from the TIM-barrel domain of one monomer and a highly conserved loop in the β-sandwich domain of the other monomer. The PLP cofactor is recognized by hydrogen-bonding, π-stacking and van der Waals interactions.

PubMed: 21139196
DOI: 10.1107/S1744309110040649

Experimental method

X-RAY DIFFRACTION (3.1 Å)