4HPV

Crystal structure of S-Adenosylmethionine synthetase from Sulfolobus solfataricus

4HPV の概要

• エントリーDOI: 10.2210/pdb4hpv/pdb
• 関連するPDBエントリー: 4K0B 4L2Z 4L7I
• 分子名称: S-adenosylmethionine synthase (2 entities in total)
• 機能のキーワード: structural genomics, psi-biology, protein structure initiative, enzyme discovery for natural product biosynthesis, natpro, transferase
• 由来する生物種: Sulfolobus solfataricus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90661.37

構造登録者

Wang, F.,Hurley, K.A.,Helmich, K.E.,Singh, S.,Bingman, C.A.,Thorson, J.S.,Phillips Jr., G.N.,Enzyme Discovery for Natural Product Biosynthesis (NatPro) (登録日: 2012-10-24, 公開日: 2012-11-14, 最終更新日: 2017-11-15)

主引用文献

Wang, F.,Singh, S.,Zhang, J.,Huber, T.D.,Helmich, K.E.,Sunkara, M.,Hurley, K.A.,Goff, R.D.,Bingman, C.A.,Morris, A.J.,Thorson, J.S.,Phillips, G.N.
Understanding molecular recognition of promiscuity of thermophilic methionine adenosyltransferase sMAT from Sulfolobus solfataricus.
Febs J., 281:4224-4239, 2014

PubMed Abstract: Methionine adenosyltransferase (MAT) is a family of enzymes that utilizes ATP and methionine to produce S-adenosylmethionine (AdoMet), the most crucial methyl donor in the biological methylation of biomolecules and bioactive natural products. Here, we report that the MAT from Sulfolobus solfataricus (sMAT), an enzyme from a poorly explored class of the MAT family, has the ability to produce a range of differentially alkylated AdoMet analogs in the presence of non-native methionine analogs and ATP. To investigate the molecular basis for AdoMet analog production, we have crystallized the sMAT in the AdoMet bound, S-adenosylethionine (AdoEth) bound and unbound forms. Notably, among these structures, the AdoEth bound form offers the first MAT structure containing a non-native product, and cumulatively these structures add new structural insight into the MAT family and allow for detailed active site comparison with its homologs in Escherichia coli and human. As a thermostable MAT structure from archaea, the structures herein also provide a basis for future engineering to potentially broaden AdoMet analog production as reagents for methyltransferase-catalyzed 'alkylrandomization' and/or the study of methylation in the context of biological processes.

PubMed: 24649856
DOI: 10.1111/febs.12784

実験手法

X-RAY DIFFRACTION (2.214 Å)