1h7d
From Proteopedia
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SOLUTION STRUCTURE OF THE 49 AA PRESEQUENCE OF 5-ALAS
Overview
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.
About this Structure
1H7D is a Single protein structure of sequence from Mus musculus. Active as 5-aminolevulinate synthase, with EC number 2.3.1.37 Full crystallographic information is available from OCA.
Reference
The solution structure and heme binding of the presequence of murine 5-aminolevulinate synthase., Goodfellow BJ, Dias JS, Ferreira GC, Henklein P, Wray V, Macedo AL, FEBS Lett. 2001 Sep 14;505(2):325-31. PMID:11566198
Page seeded by OCA on Tue Nov 20 16:26:45 2007
