1HB8

Structure of bovine Acyl-CoA binding protein in tetragonal crystal form

1HB8 の概要

• エントリーDOI: 10.2210/pdb1hb8/pdb
• 関連するPDBエントリー: 1ACA 1HB6 2ABD
• 分子名称: ACYL-COA BINDING PROTEIN, SULFATE ION (3 entities in total)
• 機能のキーワード: acyl-coenzyme a binding protein, acyl-coa, binding protein
• 由来する生物種: BOS TAURUS (BOVINE)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 30082.06

構造登録者

Zou, J.Y.,Kleywegt, G.J.,Bergfors, T.,Knudsen, J.,Jones, T.A. (登録日: 2001-04-12, 公開日: 2002-03-11, 最終更新日: 2023-12-13)

主引用文献

Van Aalten, D.M.F.,Milne, K.G.,Zou, J.Y.,Kleywegt, G.J.,Bergfors, T.,Ferguson, M.A.J.,Knudsen, J.,Jones, T.A.
Binding Site Differences Revealed by Crystal Structures of Plasmodium Falciparum and Bovine Acyl-Coa Binding Protein
J.Mol.Biol., 309:181-, 2001

PubMed Abstract: Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA molecules in the cell and plays a role in fatty acid metabolism. The biochemical properties of Plasmodium falciparum ACBP are described together with the 2.0 A resolution crystal structures of a P. falciparum ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to the NMR structures published previously; however, the bovine and parasite ACBP structures are less similar. The parasite ACBP is shown to have a different ligand-binding pocket, leading to an acyl-CoA binding specificity different from that of bovine ACBP. Several non-conservative differences in residues that interact with the ligand were identified between the mammalian and parasite ACBPs. These, together with measured binding-specificity differences, suggest that there is a potential for the design of molecules that might selectively block the acyl-CoA binding site.

PubMed: 11491287
DOI: 10.1006/JMBI.2001.4749

実験手法

X-RAY DIFFRACTION (2 Å)