1B7E

TRANSPOSASE INHIBITOR

1B7E の概要

• エントリーDOI: 10.2210/pdb1b7e/pdb
• 分子名称: PROTEIN (TRANSPOSASE INHIBITOR PROTEIN FROM TN5), 2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride (3 entities in total)
• 機能のキーワード: transposase, polynucleotidyl transferase, hydrolase, transferase inhibitor
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48503.14

構造登録者

Davies, D.R.,Braam, L.M.,Reznikoff, W.S.,Rayment, I. (登録日: 1999-01-22, 公開日: 1999-04-21, 最終更新日: 2024-05-22)

主引用文献

Davies, D.R.,Braam, L.M.,Reznikoff, W.S.,Rayment, I.
The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9A resolution.
J.Biol.Chem., 274:11904-11913, 1999

PubMed Abstract: Transposon Tn5 employs a unique means of self-regulation by expressing a truncated version of the transposase enzyme that acts as an inhibitor. The inhibitor protein differs from the full-length transposase only by the absence of the first 55 N-terminal amino acid residues. It contains the catalytic active site of transposase and a C-terminal domain involved in protein-protein interactions. The three-dimensional structure of Tn5 inhibitor determined to 2.9-A resolution is reported here. A portion of the protein fold of the catalytic core domain is similar to the folds of human immunodeficiency virus-1 integrase, avian sarcoma virus integrase, and bacteriophage Mu transposase. The Tn5 inhibitor contains an insertion that extends the beta-sheet of the catalytic core from 5 to 9 strands. All three of the conserved residues that make up the "DDE" motif of the active site are visible in the structure. An arginine residue that is strictly conserved among the IS4 family of bacterial transposases is present at the center of the active site, suggesting a catalytic motif of "DDRE." A novel C-terminal domain forms a dimer interface across a crystallographic 2-fold axis. Although this dimer represents the structure of the inhibited complex, it provides insight into the structure of the synaptic complex.

PubMed: 10207011
DOI: 10.1074/jbc.274.17.11904

実験手法

X-RAY DIFFRACTION (2.9 Å)