4H0P

Crystal Structure of Acetate Kinase from Cryptococcus neoformans

4H0P の概要

• エントリーDOI: 10.2210/pdb4h0p/pdb
• 関連するPDBエントリー: 4H0O
• 分子名称: acetate kinase (2 entities in total)
• 機能のキーワード: atp-dependent acetate kinase, askha (acetate and sugar kinase, hsc70, actin) superfamily, ribonuclease h-like fold, transferase
• 由来する生物種: Cryptococcus neoformans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96349.35

構造登録者

Thaker, T.M.,Iverson, T.M. (登録日: 2012-09-09, 公開日: 2012-12-05, 最終更新日: 2023-09-13)

主引用文献

Thaker, T.M.,Tanabe, M.,Fowler, M.L.,Preininger, A.M.,Ingram-Smith, C.,Smith, K.S.,Iverson, T.M.
Crystal structures of acetate kinases from the eukaryotic pathogens Entamoeba histolytica and Cryptococcus neoformans.
J.Struct.Biol., 181:185-189, 2013

PubMed Abstract: Acetate kinases (ACKs) are members of the acetate and sugar kinase/hsp70/actin (ASKHA) superfamily and catalyze the reversible phosphorylation of acetate, with ADP/ATP the most common phosphoryl acceptor/donor. While prokaryotic ACKs have been the subject of extensive biochemical and structural characterization, there is a comparative paucity of information on eukaryotic ACKs, and prior to this report, no structure of an ACK of eukaryotic origin was available. We determined the structures of ACKs from the eukaryotic pathogens Entamoeba histolytica and Cryptococcus neoformans. Each active site is located at an interdomain interface, and the acetate and phosphate binding pockets display sequence and structural conservation with their prokaryotic counterparts. Interestingly, the E. histolytica ACK has previously been shown to be pyrophosphate (PP(i))-dependent, and is the first ACK demonstrated to have this property. Examination of its structure demonstrates how subtle amino acid substitutions within the active site have converted cosubstrate specificity from ATP to PP(i) while retaining a similar backbone conformation. Differences in the angle between domains surrounding the active site suggest that interdomain movement may accompany catalysis. Taken together, these structures are consistent with the eukaryotic ACKs following a similar reaction mechanism as is proposed for the prokaryotic homologs.

PubMed: 23159802
DOI: 10.1016/j.jsb.2012.11.001

実験手法

X-RAY DIFFRACTION (1.894 Å)