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3GPM

Structure of the trimeric form of the E113G PCNA mutant protein

3GPM の概要
エントリーDOI10.2210/pdb3gpm/pdb
関連するPDBエントリー3GPN
分子名称Proliferating cell nuclear antigen (1 entity in total)
機能のキーワードdna damage, dna repair, dna replication, dna-binding, isopeptide bond, nucleus, ubl conjugation, dna binding protein
由来する生物種Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
細胞内の位置Nucleus: P15873
タンパク質・核酸の鎖数1
化学式量合計28871.99
構造登録者
Freudenthal, B.D.,Gakhar, L.,Ramaswamy, S.,Washington, M.T. (登録日: 2009-03-23, 公開日: 2009-06-16, 最終更新日: 2023-09-06)
主引用文献Freudenthal, B.D.,Gakhar, L.,Ramaswamy, S.,Washington, M.T.
A charged residue at the subunit interface of PCNA promotes trimer formation by destabilizing alternate subunit interactions.
Acta Crystallogr.,Sect.D, 65:560-566, 2009
Cited by
PubMed Abstract: Eukaryotic proliferating cell nuclear antigen (PCNA) is an essential replication accessory factor that interacts with a variety of proteins involved in DNA replication and repair. Each monomer of PCNA has an N-terminal domain A and a C-terminal domain B. In the structure of the wild-type PCNA protein, domain A of one monomer interacts with domain B of a neighboring monomer to form a ring-shaped trimer. Glu113 is a conserved residue at the subunit interface in domain A. Two distinct X-ray crystal structures have been determined of a mutant form of PCNA with a substitution at this position (E113G) that has previously been studied because of its effect on translesion synthesis. The first structure was the expected ring-shaped trimer. The second structure was an unanticipated nontrimeric form of the protein. In this nontrimeric form, domain A of one PCNA monomer interacts with domain A of a neighboring monomer, while domain B of this monomer interacts with domain B of a different neighboring monomer. The B-B interface is stabilized by an antiparallel beta-sheet and appears to be structurally similar to the A-B interface observed in the trimeric form of PCNA. The A-A interface, in contrast, is primarily stabilized by hydrophobic interactions. Because the E113G substitution is located on this hydrophobic surface, the A-A interface should be less favorable in the case of the wild-type protein. This suggests that the side chain of Glu113 promotes trimer formation by destabilizing these possible alternate subunit interactions.
PubMed: 19465770
DOI: 10.1107/S0907444909011329
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.8 Å)
構造検証レポート
Validation report summary of 3gpm
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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