3rid: Difference between revisions
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< | ==X-ray structure of the C-terminal swapped dimer of P114A variant of Ribonuclease A== | ||
<StructureSection load='3rid' size='340' side='right'caption='[[3rid]], [[Resolution|resolution]] 2.18Å' scene=''> | |||
== Structural highlights == | |||
or the | <table><tr><td colspan='2'>[[3rid]] is a 4 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=3RID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RID 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]] 2.18Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CGP:2-DEOXYCYTIDINE-2-DEOXYGUANOSINE-3,5-MONOPHOSPHATE'>CGP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3rid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rid OCA], [https://pdbe.org/3rid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rid RCSB], [https://www.ebi.ac.uk/pdbsum/3rid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rid ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RNAS1_BOVIN RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.<ref>PMID:7479688</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
3D domain swapping is the process by which two or more protein molecules exchange part of their structure to form intertwined dimers or higher oligomers. Bovine pancreatic ribonuclease (RNase A) is able to swap the N-terminal alpha-helix (residues 1-13) and/or the C-terminal beta-strand (residues 116-124), thus forming a variety of oligomers, including two different dimers. Cis-trans isomerization of the Asn113-Pro114 peptide group was observed when the protein formed the C-terminal swapped dimer. To study the effect of the substitution of Pro114 on the swapping process of RNase A, we have prepared and characterized the P114A monomeric and dimeric variants of the enzyme. In contrast with previous reports, the crystal structure and NMR data on the monomer reveals a mixed cis-trans conformation for the Asn113-Ala114 peptide group, whereas the X-ray structure of the C-terminal swapped dimer of the variant is very close to that of the corresponding dimer of RNase A. The mutation at the C-terminus affects the capability of the N-terminal alpha-helix to swap and the stability of both dimeric forms. The present results underscore the importance of the hydration shell in determining the cross-talk between the chain termini in the swapping process of RNase A. | |||
Chain termini cross-talk in the swapping process of bovine pancreatic ribonuclease.,Merlino A, Picone D, Ercole C, Balsamo A, Sica F Biochimie. 2012 Jan 17. PMID:22273774<ref>PMID:22273774</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3rid" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Balsamo | [[Category: Balsamo A]] | ||
[[Category: Mazzarella | [[Category: Mazzarella L]] | ||
[[Category: Merlino | [[Category: Merlino A]] | ||
[[Category: Sica | [[Category: Sica F]] | ||
Latest revision as of 20:17, 1 November 2023
X-ray structure of the C-terminal swapped dimer of P114A variant of Ribonuclease AX-ray structure of the C-terminal swapped dimer of P114A variant of Ribonuclease A
Structural highlights
FunctionRNAS1_BOVIN Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1] Publication Abstract from PubMed3D domain swapping is the process by which two or more protein molecules exchange part of their structure to form intertwined dimers or higher oligomers. Bovine pancreatic ribonuclease (RNase A) is able to swap the N-terminal alpha-helix (residues 1-13) and/or the C-terminal beta-strand (residues 116-124), thus forming a variety of oligomers, including two different dimers. Cis-trans isomerization of the Asn113-Pro114 peptide group was observed when the protein formed the C-terminal swapped dimer. To study the effect of the substitution of Pro114 on the swapping process of RNase A, we have prepared and characterized the P114A monomeric and dimeric variants of the enzyme. In contrast with previous reports, the crystal structure and NMR data on the monomer reveals a mixed cis-trans conformation for the Asn113-Ala114 peptide group, whereas the X-ray structure of the C-terminal swapped dimer of the variant is very close to that of the corresponding dimer of RNase A. The mutation at the C-terminus affects the capability of the N-terminal alpha-helix to swap and the stability of both dimeric forms. The present results underscore the importance of the hydration shell in determining the cross-talk between the chain termini in the swapping process of RNase A. Chain termini cross-talk in the swapping process of bovine pancreatic ribonuclease.,Merlino A, Picone D, Ercole C, Balsamo A, Sica F Biochimie. 2012 Jan 17. PMID:22273774[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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