3LN8
The X-ray structure of Zf-RNase-1 from a new crystal form at pH 7.3
Summary for 3LN8
Entry DOI | 10.2210/pdb3ln8/pdb |
Related | 2VQ8 2VQ9 3LJD 3LJE |
Descriptor | HYDROLASE, SULFATE ION (3 entities in total) |
Functional Keywords | angiogenins, fish rnases, hydrolase |
Biological source | Danio Rerio (zebrafish) |
Total number of polymer chains | 2 |
Total formula weight | 29667.37 |
Authors | Russo Krauss, I.,Merlino, A.,Mazzarella, L.,Sica, F. (deposition date: 2010-02-02, release date: 2010-12-08, Last modification date: 2023-09-06) |
Primary citation | Pizzo, E.,Merlino, A.,Turano, M.,Russo Krauss, I.,Coscia, F.,Zanfardino, A.,Varcamonti, M.,Furia, A.,Giancola, C.,Mazzarella, L.,Sica, F.,D'Alessio, G. A new RNase sheds light on the RNase/angiogenin subfamily from zebrafish. Biochem.J., 433:345-355, 2010 Cited by PubMed Abstract: Recently, extracellular RNases of the RNase A superfamily, with the characteristic CKxxNTF sequence signature, have been identified in fish. This has led to the recognition that these RNases are present in the whole vertebrate subphylum. In fact, they comprise the only enzyme family unique to vertebrates. Four RNases from zebrafish (Danio rerio) have been previously reported and have a very low RNase activity; some of these are endowed, like human angiogenin, with powerful angiogenic and bactericidal activities. In the present paper, we report the three-dimensional structure, the thermodynamic behaviour and the biological properties of a novel zebrafish RNase, ZF-RNase-5. The investigation of its structural and functional properties, extended to all other subfamily members, provides an inclusive description of the whole zebrafish RNase subfamily. PubMed: 21050179DOI: 10.1042/BJ20100892 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.61 Å) |
Structure validation
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