1og4 | pdb_00001og4

Crystal Structure of the Eucaryotic Mono-ADP-Ribosyltransferase ART2.2 Mutant E189A in Complex with NADH

spinqualitylabelsall models 1og4, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1og4 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 2.6Å Ligands: NAI 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 structures of beta-methylenethiazole-4-carboxamide adenine dinucleotide (TAD), NAD(+), and NADH as bound to ecto-ADP-ribosyltransferase 2.2 from rat and to its mutants E189I and E189A, respectively, have been established. The positions and conformations of NAD(+) and its analogues agree in general with those in other ADP-ribosyltransferases. The kinetic constants for NAD(+) hydrolysis were determined by RP-HPLC. The specific activity amounts to 26 units/mg, which is 6000-fold higher than a previously reported rate and 500-fold higher than the hydrolysis rates of other ADP-ribosyltransferases, confirming that hydrolysis is the major function of this enzyme. On the basis of structures and mutant activities, a catalytic mechanism is proposed. The known auto-ADP-ribosylation of the enzyme at the suggested position R184 is supported by one of the crystal structures where the nucleophile position is occupied by an Neta atom of this arginine which in turn is backed up by the base E159. Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat.,Ritter H, Koch-Nolte F, Marquez VE, Schulz GE Biochemistry. 2003 Sep 2;42(34):10155-62. PMID:12939142 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA