3H86

Crystal structure of adenylate kinase from Methanococcus maripaludis

Summary for 3H86

• Entry DOI: 10.2210/pdb3h86/pdb
• Related: 1KHT 1KI9
• Descriptor: Adenylate kinase, BIS(ADENOSINE)-5'-PENTAPHOSPHATE (3 entities in total)
• Functional Keywords: mesophile, kinase, adenylate kinase, phosphotransferase, atp-binding, cytoplasm, nucleotide-binding, transferase
• Biological source: Methanococcus maripaludis
• Cellular location: Cytoplasm : Q6LYG0
• Total number of polymer chains: 4
• Total formula weight: 88038.44

Authors

Milya, D.G.,Yousif, S. (deposition date: 2009-04-28, release date: 2009-10-06, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)