3RID

X-ray structure of the C-terminal swapped dimer of P114A variant of Ribonuclease A

3RID の概要

• エントリーDOI: 10.2210/pdb3rid/pdb
• 分子名称: Ribonuclease pancreatic, 2'-DEOXYCYTIDINE-2'-DEOXYGUANOSINE-3',5'-MONOPHOSPHATE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: ribonuclease fold, hydrolase
• 由来する生物種: Bos taurus (bovine)
• 細胞内の位置: Secreted: P61823
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 57334.73

構造登録者

Merlino, A.,Balsamo, A.,Mazzarella, L.,Sica, F. (登録日: 2011-04-13, 公開日: 2012-02-15, 最終更新日: 2024-10-16)

主引用文献

Merlino, A.,Picone, D.,Ercole, C.,Balsamo, A.,Sica, F.
Chain termini cross-talk in the swapping process of bovine pancreatic ribonuclease.
Biochimie, 94:1108-1118, 2012

PubMed Abstract: 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 α-helix (residues 1-13) and/or the C-terminal β-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 α-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.

PubMed: 22273774
DOI: 10.1016/j.biochi.2012.01.010

実験手法

X-RAY DIFFRACTION (2.18 Å)