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Literature summary extracted from

  • Chin, K.; Yang, C.; Chou, C.; Wang, A.H.; Chou, S.
    The crystal structure of XC847 from Xanthomonas campestris: A 3-5 oligoribonuclease of DnaQ fold family with a novel opposingly shifted helix (2006), Proteins Struct. Funct. Bioinform., 65, 1036-1040.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.13.3 into pMCSG7 vector Xanthomonas campestris

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.13.3 by sitting-drop vapor diffusion method, to a resolution of 2.1 A, orn monomer comprises 9 alpha-helices and 5 beta-strands, helix H is oriented opposingly from similar helices in all reported 3'-5' DNases discovered so far, possibly to prevent steric hindrance of accommodating oligoribonucleotide substrates. Amino acids Leu135, Leu143, Ile140, and Leu174 form a hydrophobic cluster, side chains of Glu142/Arg133 and Thr139/Asp136 form salt bridges and H-bonds in the dimer interface, while side chains of Arg145, and Lys157 interact with the ribose 2'-OH or phosphate oxygen atoms of U5 substrates Xanthomonas campestris

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.13.3 Mg2+ one magnesium ion, coordinating well with the DEDDh active site carboxylate groups of Asp15, Glu17, Asp166, and the oxygen atom of U51Op group Xanthomonas campestris

Organism

EC Number Organism UniProt Comment Textmining
3.1.13.3 Xanthomonas campestris
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.13.3 more than 99% pure Xanthomonas campestris

Subunits

EC Number Subunits Comment Organism
3.1.13.3 homodimer crystallography Xanthomonas campestris

Synonyms

EC Number Synonyms Comment Organism
3.1.13.3 XC847
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Xanthomonas campestris

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.13.3 additional information
-
active site highly acidic and substrate binding site highly basic Xanthomonas campestris