3PUG

Haloferax volcanii Malate Synthase Native at 3mM Glyoxylate

3PUG の概要

• エントリーDOI: 10.2210/pdb3pug/pdb
• 関連するPDBエントリー: 3OYX 3OYZ
• 分子名称: Malate Synthase, GLYOXYLIC ACID, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: tim barrel, transferase
• 由来する生物種: Haloferax volcanii
• 細胞内の位置: Cytoplasm : D4GTL2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48463.39

構造登録者

Howard, B.R.,Bracken, C.D.,Neighbor, A.M.,Thomas, G.C.,Lamlenn, K.K.,Schubert, H.L.,Whitby, F.G. (登録日: 2010-12-04, 公開日: 2011-06-01, 最終更新日: 2024-02-21)

主引用文献

Bracken, C.D.,Neighbor, A.M.,Lamlenn, K.K.,Thomas, G.C.,Schubert, H.L.,Whitby, F.G.,Howard, B.R.
Crystal structures of a halophilic archaeal malate synthase from Haloferax volcanii and comparisons with isoforms A and G.
Bmc Struct.Biol., 11:23-23, 2011

PubMed Abstract: Malate synthase, one of the two enzymes unique to the glyoxylate cycle, is found in all three domains of life, and is crucial to the utilization of two-carbon compounds for net biosynthetic pathways such as gluconeogenesis. In addition to the main isoforms A and G, so named because of their differential expression in E. coli grown on either acetate or glycolate respectively, a third distinct isoform has been identified. These three isoforms differ considerably in size and sequence conservation. The A isoform (MSA) comprises ~530 residues, the G isoform (MSG) is ~730 residues, and this third isoform (MSH-halophilic) is ~430 residues in length. Both isoforms A and G have been structurally characterized in detail, but no structures have been reported for the H isoform which has been found thus far only in members of the halophilic Archaea.

PubMed: 21569248
DOI: 10.1186/1472-6807-11-23

実験手法

X-RAY DIFFRACTION (2.7 Å)