1ZIN

ADENYLATE KINASE WITH BOUND AP5A

1ZIN の概要

• エントリーDOI: 10.2210/pdb1zin/pdb
• 分子名称: ADENYLATE KINASE, ZINC ION, BIS(ADENOSINE)-5'-PENTAPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: phosphotransferase, zinc finger
• 由来する生物種: Geobacillus stearothermophilus
• 細胞内の位置: Cytoplasm : P27142
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25156.64

構造登録者

Berry, M.B.,Phillips Jr., G.N. (登録日: 1996-06-07, 公開日: 1997-06-16, 最終更新日: 2024-04-03)

主引用文献

Berry, M.B.,Phillips Jr., G.N.
Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mg2+ Ap5A, and Mn2+ Ap5A reveal an intermediate lid position and six coordinate octahedral geometry for bound Mg2+ and Mn2+.
Proteins, 32:276-288, 1998

PubMed Abstract: Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mn2+ Ap5A, and Mg2+ Ap5A have been determined by X-ray crystallography to resolutions of 1.6 A, 1.85 A, and 1.96 A, respectively. The protein's lid domain is partially open, being both rotated and translated away from bound Ap5A. The flexibility of the lid domain in the ternary state and its ability to transfer force directly to the the active site is discussed in light of our proposed entropic mechanism for catalytic turnover. The bound Zn2+ atom is demonstrably structural in nature, with no contacts other than its ligating cysteine residues within 5 A. The B. stearothermophilus adenylate kinase lid appears to be a truncated zinc finger domain, lacking the DNA binding finger, which we have termed a zinc knuckle domain. In the Mg2+ Ap5A and Mn2+ Ap5A structures, Mg2+ and Mn2+ demonstrate six coordinate octahedral geometry. The interactions of the Mg2+-coordinated water molecules with the protein and Ap5A phosphate chain demonstrate their involvement in catalyzing phosphate transfer. The protein selects for beta-y (preferred by Mg2+) rather than alpha-gamma (preferred by Mn2+) metal ion coordination by forcing the ATP phosphate chain to have an extended conformation.

PubMed: 9715904
DOI: 10.1002/(SICI)1097-0134(19980815)32:3<276::AID-PROT3>3.0.CO;2-G

実験手法

X-RAY DIFFRACTION (1.6 Å)