1gy0

crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; CRYSTAL FORM C (P3121)

spinqualitylabelsall models 1gy0, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gy0 is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.08Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NAR2B_RAT Has both NAD(+) glycohydrolase and ADP-ribosyltransferase activity (to a lesser extent). 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 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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