2o3b | pdb_00002o3b

Crystal structure complex of Nuclease A (NucA) with intra-cellular inhibitor NuiA

spinqualitylabelsall models 2o3b, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2o3b is a 2 chain structure with sequence from Anabaena 7120. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MES, MG, NI Related: 1zm8 Gene: nucA (Anabaena 7120), nuiA (Anabaena 7120) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NUCA_NOSS1] Catalyzes the degradation of both RNA and DNA; has the potential to act as an endonuclease. 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 Nonspecific, extracellular nucleases have received enhanced attention recently as a consequence of the critical role that these enzymes can play in infectivity by overcoming the host neutrophil defense system. The activity of the cyanobacterial nuclease NucA, a member of the betabetaalpha Me superfamily, is controlled by the specific nuclease inhibitor, NuiA. Here we report the 2.3-A resolution crystal structure of the NucA-NuiA complex, showing that NucA inhibition by NuiA involves an unusual divalent metal ion bridge that connects the nuclease with its inhibitor. The C-terminal Thr-135(NuiA) hydroxyl oxygen is directly coordinated with the catalytic Mg(2+) of the nuclease active site, and Glu-24(NuiA) also extends into the active site, mimicking the charge of a scissile phosphate. NuiA residues Asp-75 and Trp-76 form a second interaction site, contributing to the strength and specificity of the interaction. The crystallographically defined interface is shown to be consistent with results of studies using site-directed NuiA mutants. This mode of inhibition differs dramatically from the exosite mechanism of inhibition seen with the DNase colicins E7/E9 and from other nuclease-inhibitor complexes that have been studied. The structure of this complex provides valuable insights for the development of inhibitors for related nonspecific nucleases that share the DRGH active site motif such as the Streptococcus pneumoniae nuclease EndA, which mediates infectivity of this pathogen, and mitochondrial EndoG, which is involved in recombination and apoptosis. The nuclease a-inhibitor complex is characterized by a novel metal ion bridge.,Ghosh M, Meiss G, Pingoud AM, London RE, Pedersen LC J Biol Chem. 2007 Feb 23;282(8):5682-90. Epub 2006 Nov 30. PMID:17138564 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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