1E5M

Beta ketoacyl acyl carrier protein synthase II (KASII) from Synechocystis sp.

1E5M の概要

• エントリーDOI: 10.2210/pdb1e5m/pdb
• 分子名称: BETA KETOACYL ACYL CARRIER PROTEIN SYNTHASE II (2 entities in total)
• 機能のキーワード: condensing enzyme, biosynthetic role, carbon-carbon bond formation
• 由来する生物種: SYNECHOCYSTIS SP.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44047.96

構造登録者

Moche, M.,Edwards, P.,Dehesh, K.,Lindqvist, Y. (登録日: 2000-07-27, 公開日: 2001-01-16, 最終更新日: 2023-12-13)

主引用文献

Moche, M.,Dehesh, K.,Edwards, P.,Lindqvist, Y.
The Crystal Structure of Beta-Ketoacyl-Acyl Carrier Protein Synthase II from Synechocystis Sp. At 1.54 A Resolution and its Relationship to Other Condensing Enzymes
J.Mol.Biol., 305:491-, 2001

PubMed Abstract: Condensing enzymes, catalyzing the formation of carbon-carbon bonds in several biosynthetic pathways, have lately been recognized as potential drug targets against cancer and tuberculosis, as crucial for combinatorial biosynthesis of antibiotics and related compounds, and as determinants of plant oil composition. beta-Ketoacyl-ACP synthases (KAS) are the condensing enzymes present in the fatty acid biosynthesis pathway and are able to elongate an acyl chain bound to either co-enzyme A (CoA) or acyl carrier protein (ACP) with a two-carbon unit derived from malonyl-ACP. Several isoforms of KAS with different substrate specificity are present in most species. We have determined the crystal structure of KAS II from Synechocystis sp. PCC 6803 to 1.54 A resolution giving a detailed description of the active site geometry. In order to analyze the structure-function relationships in this class of enzymes in more detail, we have compared all presently known three-dimensional structures of condensing enzymes from different pathways. The comparison reveals that these enzymes can be divided into three structural and functional classes. This classification can be related to variations in the catalytic mechanism and the set of residues in the catalytic site, e.g. due to differences in the nature of the second substrate providing the two-carbon elongation unit. The variation in the acyl-carrier (ACP or CoA) specificity might also be connected to this classification and residues involved in ACP binding in structure class 2 can be suggested based on the comparison. Finally, the two subunits in the dimer contribute differently to formation of the substrate binding-pocket in the three structural classes.

PubMed: 11152607
DOI: 10.1006/JMBI.2000.4272

実験手法

X-RAY DIFFRACTION (1.54 Å)