1gxz
From Proteopedia
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CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE ART2.2; CRYSTAL FORM B (P212121)
Overview
The mammalian extracellular ADP-ribosyl transferases ART1 through ART5 are, sequence-related to each other. Among them ART2 is involved in immuno, regulation. The variant ART2.2 was expressed in the periplasm of, Escherichia coli and crystallized. Its structure was determined by X-ray, diffraction at 1.7A resolution in one crystal form and at slightly lower, resolutions in two others. The active center was indicated by a ligated, nicotinamide analogue, which also revealed a small induced-fit. The, centerpiece of the chainfold of ART2.2 agrees with those of all bacterial, ADP-ribosyl transferases. This correspondence and the nicotinamide, position were used to model the binding structure of the whole substrate, NAD(+) at ART2.2. Two of the bacterial enzymes are structurally more, closely related to ART2.2 while the others are more closely related to the, eukaryotic poly(ADP-ribosyl)polymerase. This splits the ADP-ribosyl, transferases into two distinct subfamilies. A special feature of ART2.2 is, its long N-terminal extension and two disulfide bridges that are far away, from the active center. They stabilize the protein against denaturation, and presumably also against shearing forces parallel with the membrane, where ART2.2 is anchored.
About this Structure
1GXZ is a Single protein structure of sequence from Rattus norvegicus with BRT as ligand. Active as NAD(P)(+)--protein-arginine ADP-ribosyltransferase, with EC number 2.4.2.31 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Structure of the ecto-ADP-ribosyl transferase ART2.2 from rat., Mueller-Dieckmann C, Ritter H, Haag F, Koch-Nolte F, Schulz GE, J Mol Biol. 2002 Sep 27;322(4):687-96. PMID:12270706
Page seeded by OCA on Mon Nov 5 16:22:40 2007
