2UZF

Crystal structure of Staphylococcus aureus 1,4-dihydroxy-2-naphthoyl CoA synthase (MenB) in complex with acetoacetyl CoA

2UZF の概要

• エントリーDOI: 10.2210/pdb2uzf/pdb
• 分子名称: NAPHTHOATE SYNTHASE, ACETOACETYL-COENZYME A (3 entities in total)
• 機能のキーワード: lyase, menaquinone biosynthesis
• 由来する生物種: STAPHYLOCOCCUS AUREUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61776.77

構造登録者

Ulaganathan, V.,Buetow, L.,Hunter, W.N. (登録日: 2007-04-27, 公開日: 2007-11-13, 最終更新日: 2023-12-13)

主引用文献

Ulaganathan, V.,Agacan, M.F.,Buetow, L.,Tulloch, L.B.,Hunter, W.N.
Structure of Staphylococcus Aureus1,4-Dihydroxy-2-Naphthoyl-Coa Synthase (Menb) in Complex with Acetoacetyl-Coa.
Acta Crystallogr.,Sect.F, 63:908-, 2007

PubMed Abstract: Vitamin K(2), or menaquinone, is an essential cofactor for many organisms and the enzymes involved in its biosynthesis are potential antimicrobial drug targets. One of these enzymes, 1,4-dihydroxy-2-naphthoyl-CoA synthase (MenB) from the pathogen Staphylococcus aureus, has been obtained in recombinant form and its quaternary structure has been analyzed in solution. Cubic crystals of the enzyme allowed a low-resolution structure (2.9 A) to be determined. The asymmetric unit consists of two subunits and a crystallographic threefold axis of symmetry generates a hexamer consistent with size-exclusion chromatography. Analytical ultracentrifugation indicates the presence of six states in solution, monomeric through to hexameric, with the dimer noted as being particularly stable. MenB displays the crotonase-family fold with distinct N- and C-terminal domains and a flexible segment of structure around the active site. The smaller C-terminal domain plays an important role in oligomerization and also in substrate binding. The presence of acetoacetyl-CoA in one of the two active sites present in the asymmetric unit indicates how part of the substrate binds and facilitates comparisons with the structure of Mycobacterium tuberculosis MenB.

PubMed: 18007038
DOI: 10.1107/S1744309107047720

実験手法

X-RAY DIFFRACTION (2.9 Å)