3H86

Crystal structure of adenylate kinase from Methanococcus maripaludis

3H86 の概要

• エントリーDOI: 10.2210/pdb3h86/pdb
• 関連するPDBエントリー: 1KHT 1KI9
• 分子名称: Adenylate kinase, BIS(ADENOSINE)-5'-PENTAPHOSPHATE (3 entities in total)
• 機能のキーワード: mesophile, kinase, adenylate kinase, phosphotransferase, atp-binding, cytoplasm, nucleotide-binding, transferase
• 由来する生物種: Methanococcus maripaludis
• 細胞内の位置: Cytoplasm : Q6LYG0
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 88038.44

構造登録者

Milya, D.G.,Yousif, S. (登録日: 2009-04-28, 公開日: 2009-10-06, 最終更新日: 2023-11-29)

主引用文献

Davlieva, M.,Shamoo, Y.
Crystal structure of a trimeric archaeal adenylate kinase from the mesophile Methanococcus maripaludis with an unusually broad functional range and thermal stability.
Proteins, 78:357-364, 2009

PubMed Abstract: The structure of the trimeric adenylate kinase from the Archaebacteria Methanococcus mariplaludis (AK(MAR)) has been solved to 2.5-A resolution and the temperature dependent stability and kinetics of the enzyme measured. The K(M) and V(max) of AK(MAR) exhibit only modest temperature dependence from 30 degrees -60 degrees C. Although M. mariplaludis is a mesophile with a maximum growth temperature of 43 degrees C, AK(MAR) has a very broad functional range and stability (T(m) = 74.0 degrees C) that are more consistent with a thermophilic enzyme with high thermostability and exceptional activity over a wide range of temperatures, suggesting that this microbe may have only recently invaded a mesophilic niche and has yet to fully adapt. A comparison of the Local Structural Entropy (LSE) for AK(MAR) to the related adenylate kinases from the mesophile Methanococcus voltae and thermophile Methanococcus thermolithotrophicus show that changes in LSE are able to fully account for the intermediate stability of AK(MAR) and highlights a general mechanism for protein adaptation in this class of enzymes.

PubMed: 19731371
DOI: 10.1002/prot.22549

実験手法

X-RAY DIFFRACTION (2.5 Å)