4n4c: Difference between revisions
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== | ==Crystal structure of the C-terminal swapped dimer of a Bovine seminal ribonuclease mutant== | ||
[[http://www.uniprot.org/uniprot/RNS_BOVIN RNS_BOVIN | <StructureSection load='4n4c' size='340' side='right'caption='[[4n4c]], [[Resolution|resolution]] 2.48Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4n4c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N4C FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.48Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4c OCA], [https://pdbe.org/4n4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n4c RCSB], [https://www.ebi.ac.uk/pdbsum/4n4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4c ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RNS_BOVIN RNS_BOVIN] This enzyme hydrolyzes both single- and double-stranded RNA. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bovine seminal ribonuclease (BS-RNase) acquires an interesting anti-tumor activity associated with the swapping on the N-termini. The first direct experimental evidence on the formation of a C-terminal swapped dimer (C-dimer) obtained from the monomeric derivative of BS-RNase, although under non-native conditions, is here reported. The X-ray model of this dimer reveals a quaternary structure different from that of the C-dimer of RNase A, due to the presence of three mutations in the hinge peptide 111-116. The mutations increase the hinge peptide flexibility and decrease the stability of the C-dimer against dissociation. The biological implications of the structural data are also discussed. | |||
The multiple forms of Bovine Seminal Ribonuclease: structure and stability of a C-terminal swapped dimer.,Sica F, Pica A, Merlino A, Krauss IR, Ercole C, Picone D FEBS Lett. 2013 Oct 15. pii: S0014-5793(13)00745-X. doi:, 10.1016/j.febslet.2013.10.003. PMID:24140346<ref>PMID:24140346</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
[[ | <div class="pdbe-citations 4n4c" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Merlino | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
[[Category: Pica | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Merlino A]] | |||
[[Category: Pica A]] | |||
[[Category: Russo Krauss I]] | |||
[[Category: Sica F]] | |||
Latest revision as of 19:47, 20 September 2023
Crystal structure of the C-terminal swapped dimer of a Bovine seminal ribonuclease mutantCrystal structure of the C-terminal swapped dimer of a Bovine seminal ribonuclease mutant
Structural highlights
FunctionRNS_BOVIN This enzyme hydrolyzes both single- and double-stranded RNA. Publication Abstract from PubMedBovine seminal ribonuclease (BS-RNase) acquires an interesting anti-tumor activity associated with the swapping on the N-termini. The first direct experimental evidence on the formation of a C-terminal swapped dimer (C-dimer) obtained from the monomeric derivative of BS-RNase, although under non-native conditions, is here reported. The X-ray model of this dimer reveals a quaternary structure different from that of the C-dimer of RNase A, due to the presence of three mutations in the hinge peptide 111-116. The mutations increase the hinge peptide flexibility and decrease the stability of the C-dimer against dissociation. The biological implications of the structural data are also discussed. The multiple forms of Bovine Seminal Ribonuclease: structure and stability of a C-terminal swapped dimer.,Sica F, Pica A, Merlino A, Krauss IR, Ercole C, Picone D FEBS Lett. 2013 Oct 15. pii: S0014-5793(13)00745-X. doi:, 10.1016/j.febslet.2013.10.003. PMID:24140346[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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