1H7D

Solution structure of the 49 aa presequence of 5-ALAS

1H7D の概要

• エントリーDOI: 10.2210/pdb1h7d/pdb
• 分子名称: AMINOLEVULINIC ACID SYNTHASE 2, ERYTHROID (1 entity in total)
• 機能のキーワード: acyltransferase, alas, presequence
• 由来する生物種: MUS MUSCULUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5102.14

構造登録者

Goodfellow, B.J.,Dias, J.S.,Ferreira, G.C.,Wray, V.,Henklein, P.,Macedo, A.L. (登録日: 2001-07-05, 公開日: 2001-10-18, 最終更新日: 2024-05-15)

主引用文献

Goodfellow, B.J.,Dias, J.S.,Ferreira, G.C.,Henklein, P.,Wray, V.,Macedo, A.L.
The Solution Structure and Heme Binding of the Presequence of Murine 5-Aminolevulinate Synthase
FEBS Lett., 505:325-, 2001

PubMed Abstract: The mitochondrial import of 5-aminolevulinate synthase (ALAS), the first enzyme of the mammalian heme biosynthetic pathway, requires the N-terminal presequence. The 49 amino acid presequence transit peptide (psALAS) for murine erythroid ALAS was chemically synthesized, and circular dichroism and (1)H nuclear magnetic resonance (NMR) spectroscopies used to determine structural elements in trifluoroethanol/H(2)O solutions and micellar environments. A well defined amphipathic alpha-helix, spanning L22 to F33, was present in psALAS in 50% trifluoroethanol. Further, a short alpha-helix, defined by A5-L8, was also apparent in the 26 amino acid N-terminus peptide, when its structure was determined in sodium dodecyl sulfate. Heme inhibition of ALAS mitochondrial import has been reported to be mediated through cysteine residues in presequence heme regulatory motifs (HRMs). A UV/visible and (1)H NMR study of hemin and psALAS indicated that a heme-peptide interaction occurs and demonstrates, for the first time, that heme interacts with the HRMs of psALAS.

PubMed: 11566198
DOI: 10.1016/S0014-5793(01)02818-6

実験手法

SOLUTION NMR