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3LJD

The X-ray structure of zebrafish RNase1 from a new crystal form at pH 4.5

Summary for 3LJD
Entry DOI10.2210/pdb3ljd/pdb
Related2VQ8 2VQ9 3LJE 3LN8
DescriptorZebrafish RNase1, SULFATE ION, ACETATE ION, ... (4 entities in total)
Functional Keywordsangiogenins, fish rnases, hydrolase
Biological sourceDanio rerio (zebrafish)
Total number of polymer chains2
Total formula weight29534.29
Authors
Russo Krauss, I.,Merlino, A.,Mazzarella, L.,Sica, F. (deposition date: 2010-01-26, release date: 2010-12-08, Last modification date: 2024-10-16)
Primary citationPizzo, 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: 21050179
DOI: 10.1042/BJ20100892
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.38 Å)
Structure validation

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