4HAC

Crystal Structure of the Mevalonate Kinase from an Archaeon Methanosarcina mazei

Summary for 4HAC

• Entry DOI: 10.2210/pdb4hac/pdb
• Descriptor: Mevalonate kinase, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: ghmp, atp binding, phosphorylation, transferase
• Biological source: Methanosarcina mazei; More
• Cellular location: Cytoplasm : Q8PW39 Q8PW39
• Total number of polymer chains: 2
• Total formula weight: 67697.55

Authors

Zhuang, N.,Lee, K.H. (deposition date: 2012-09-26, release date: 2012-12-12, Last modification date: 2024-10-30)

Primary citation

Zhuang, N.,Seo, K.H.,Chen, C.,Zhou, J.,Kim, S.W.,Lee, K.H.
Crystallization and preliminary X-ray diffraction analysis of mevalonate kinase from Methanosarcina mazei.
Acta Crystallogr.,Sect.F, 68:1560-1563, 2012

PubMed Abstract: Mevalonate kinase (MVK), which plays an important role in catalysing the biosynthesis of isoprenoid compounds derived from the mevalonate pathway, transforms mevalonate to 5-phosphomevalonate using ATP as a cofactor. Mevalonate kinase from Methanosarcina mazei (MmMVK) was expressed in Escherichia coli, purified and crystallized for structural analysis. Diffraction-quality crystals of MmMVK were obtained by the vapour-diffusion method using 0.32 M MgCl2, 0.08 M bis-tris pH 5.5, 16%(w/v) PEG 3350. The crystals belonged to space group P2(1)2(1)2, with unit-cell parameters a=97.11, b=135.92, c=46.03 Å. Diffraction data were collected to 2.08 Å resolution.

PubMed: 23192048
DOI: 10.1107/S1744309112047070

Experimental method

X-RAY DIFFRACTION (1.92 Å)