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2VQ9

RNASE ZF-3E

Summary for 2VQ9
Entry DOI10.2210/pdb2vq9/pdb
Related2VQ8
DescriptorRNASE 1, CHLORIDE ION (3 entities in total)
Functional Keywordsnuclease, evolution, hydrolase, zebrafish, polymorphism, endonuclease, ribonucleases
Biological sourceDANIO RERIO (ZEBRAFISH)
Cellular locationSecreted (By similarity): A5HAK0
Total number of polymer chains1
Total formula weight17133.05
Authors
Kazakou, K.,Holloway, D.E.,Prior, S.H.,Subramanian, V.,Acharya, K.R. (deposition date: 2008-03-12, release date: 2008-06-17, Last modification date: 2024-10-16)
Primary citationKazakou, K.,Holloway, D.E.,Prior, S.H.,Subramanian, V.,Acharya, K.R.
Ribonuclease A Homologues of the Zebrafish: Polymorphism, Crystal Structures of Two Representatives and Their Evolutionary Implications
J.Mol.Biol., 380:206-, 2008
Cited by
PubMed Abstract: The widespread and functionally varied members of the ribonuclease A (RNase A) superfamily provide an excellent opportunity to study evolutionary forces at work on a conserved protein scaffold. Representatives from the zebrafish are of particular interest as the evolutionary distance from non-ichthyic homologues is large. We conducted an exhaustive survey of available zebrafish DNA sequences and found significant polymorphism among its four known homologues. In an extension of previous nomenclature, the variants have been named RNases ZF-1a-c,-2a-d,-3a-e and-4. We present the first X-ray crystal structures of zebrafish ribonucleases, RNases ZF-1a and-3e at 1.35-and 1.85 A resolution, respectively. Structure-based clustering with ten other ribonuclease structures indicates greatest similarity to mammalian angiogenins and amphibian ribonucleases, and supports the view that all present-day ribonucleases evolved from a progenitor with three disulphide bonds. In their details, the two structures are intriguing melting-pots of features present in ribonucleases from other vertebrate classes. Whereas in RNase ZF-1a the active site is obstructed by the C-terminal segment (as observed in angiogenin), in RNase ZF-3e the same region is open (as observed in more catalytically efficient homologues). The progenitor of present-day ribonucleases is more likely to have had an obstructive C terminus, and the relatively high similarity (late divergence) of RNases ZF-1 and-3 infers that the active site unblocking event has happened independently in different vertebrate lineages.
PubMed: 18508078
DOI: 10.1016/J.JMB.2008.04.070
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

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数据于2025-06-18公开中

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