+検索条件
-Structure paper
タイトル | and human hexokinases share similar active sites but display distinct quaternary architectures. |
---|---|
ジャーナル・号・ページ | IUCrJ, Vol. 7, Issue Pt 3, Page 453-461, Year 2020 |
掲載日 | 2020年5月1日 |
著者 | Shanti Swaroop Srivastava / Joseph E Darling / Jimmy Suryadi / James C Morris / Mark E Drew / Sriram Subramaniam / |
PubMed 要旨 | Malaria is a devastating disease caused by a protozoan parasite. It affects over 300 million individuals and results in over 400 000 deaths annually, most of whom are young children under the age ...Malaria is a devastating disease caused by a protozoan parasite. It affects over 300 million individuals and results in over 400 000 deaths annually, most of whom are young children under the age of five. Hexokinase, the first enzyme in glucose metabolism, plays an important role in the infection process and represents a promising target for therapeutic intervention. Here, cryo-EM structures of two conformational states of hexokinase (PvHK) are reported at resolutions of ∼3 Å. It is shown that unlike other known hexokinase structures, PvHK displays a unique tetrameric organization (∼220 kDa) that can exist in either open or closed quaternary conformational states. Despite the resemblance of the active site of PvHK to its mammalian counterparts, this tetrameric organization is distinct from that of human hexokinases, providing a foundation for the structure-guided design of parasite-selective antimalarial drugs. |
リンク | IUCrJ / PubMed:32431829 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.3 - 3.5 Å |
構造データ | EMDB-21458, PDB-6vyf: EMDB-21459, PDB-6vyg: |
由来 |
|
キーワード | TRANSFERASE / Hexokinase |