3nzp

Crystal Structure of the Biosynthetic Arginine decarboxylase SpeA from Campylobacter jejuni, Northeast Structural Genomics Consortium Target BR53

spinqualitylabelsall models 3nzp, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3nzp is a 2 chain structure with sequence from Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: MSE, PLP, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q0PAC6_CAMJE Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 A resolution and that of Escherichia coli SpeA in complex with a sulfate ion is reported at 3.1 A resolution. The structure of the SpeA monomer contains two large domains, an N-terminal TIM-barrel domain followed by a beta-sandwich domain, as well as two smaller helical domains. The TIM-barrel and beta-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 beta-sandwich domain of the other monomer. The PLP cofactor is recognized by hydrogen-bonding, pi-stacking and van der Waals interactions. Structures of bacterial biosynthetic arginine decarboxylases.,Forouhar F, Lew S, Seetharaman J, Xiao R, Acton TB, Montelione GT, Tong L Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt, 12):1562-6. Epub 2010 Nov 16. PMID:21139196 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA