scholarly journals The 1.6 Å Crystal Structure ofMycobacterium smegmatisMshC: The Penultimate Enzyme in the Mycothiol Biosynthetic Pathway†

Biochemistry ◽  
2008 ◽  
Vol 47 (50) ◽  
pp. 13326-13335 ◽  
Author(s):  
L. W. Tremblay ◽  
F. Fan ◽  
M. W. Vetting ◽  
J. S. Blanchard
Keyword(s):  
Crystal Structure ◽  
Biosynthetic Pathway

Crystal Structure of Vancosaminyltransferase GtfD from the Vancomycin Biosynthetic Pathway:  Interactions with Acceptor and Nucleotide Ligands†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (18) ◽  
pp. 5170-5180 ◽  
Author(s):  
Anne M. Mulichak ◽  
Wei Lu ◽  
Heather C. Losey ◽  
Christopher T. Walsh ◽  
R. Michael Garavito
Keyword(s):  
Crystal Structure ◽  
Biosynthetic Pathway

scholarly journals The Arabidopsis locus AT3G03890 encodes a dimeric β-barrel protein implicated in heme degradation

2020 ◽  
Vol 477 (24) ◽  
pp. 4785-4796
Author(s):  
Jia Wang ◽  
Qi Guo ◽  
Xiaoyi Li ◽  
Xiao Wang ◽  
Lin Liu
Keyword(s):  
Crystal Structure ◽  
Recombinant Protein ◽  
Water Molecule ◽  
Heme Oxygenase ◽  
Protein Complex ◽  
Biosynthetic Pathway ◽  
Initial Step ◽  
Heme Iron ◽  
Heme Binding ◽  
New Protein

Plant tetrapyrroles, including heme and bilins, are synthesized in plastids. Heme oxygenase (HO) catalyzes the oxidative cleavage of heme to the linear tetrapyrrole biliverdin as the initial step in bilin biosynthesis. Besides the canonical α-helical HO that is conserved from prokaryotes to human, a subfamily of non-canonical dimeric β-barrel HO has been found in bacteria. In this work, we discovered that the Arabidopsis locus AT3G03890 encodes a dimeric β-barrel protein that is structurally related to the putative non-canonical HO and is located in chloroplasts. The recombinant protein was able to bind and degrade heme in a manner different from known HO proteins. Crystal structure of the heme–protein complex reveals that the heme-binding site is in the interdimer interface and the heme iron is co-ordinated by a fixed water molecule. Our results identify a new protein that may function additionally in the tetrapyrrole biosynthetic pathway.

scholarly journals Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway

Structure ◽  
1999 ◽  
Vol 7 (11) ◽  
pp. 1395-1406 ◽  
Author(s):  
Irimpan I Mathews ◽  
T Joseph Kappock ◽  
JoAnne Stubbe ◽  
Steven E Ealick
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Biosynthetic Pathway

scholarly journals Crystal Structure of Baeyer−Villiger Monooxygenase MtmOIV, the Key Enzyme of the Mithramycin Biosynthetic Pathway,

Biochemistry ◽  
2009 ◽  
Vol 48 (21) ◽  
pp. 4476-4487 ◽  
Author(s):  
Miranda P. Beam ◽  
Mary A. Bosserman ◽  
Nicholas Noinaj ◽  
Marie Wehenkel ◽  
Jürgen Rohr
Keyword(s):  
Crystal Structure ◽  
Biosynthetic Pathway ◽  
Key Enzyme

scholarly journals Crystal structure of the glycosyltransferase SnogD from the biosynthetic pathway of nogalamycin inStreptomyces nogalater

FEBS Journal ◽  
2012 ◽  
Vol 279 (17) ◽  
pp. 3251-3263 ◽  
Author(s):  
Magnus Claesson ◽  
Vilja Siitonen ◽  
Doreen Dobritzsch ◽  
Mikko Metsä-Ketelä ◽  
Gunter Schneider
Keyword(s):  
Crystal Structure ◽  
Biosynthetic Pathway

scholarly journals Inositol lipid synthesis is widespread in host-associated Bacteroidetes

2021 ◽  
Author(s):  
S. L. Heaver ◽  
H. H. Le ◽  
P. Tang ◽  
A. Baslé ◽  
J. Marles-Wright ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Biosynthetic Pathway ◽  
Inositol Phosphate ◽  
Lipid Production ◽  
Lipid Synthesis ◽  
Kinetic Studies ◽  
Human Gut ◽  
Host Interactions ◽  
Phosphatidylinositol Phosphate ◽  
Inositol Lipids

AbstractUbiquitous in eukaryotes, inositol lipids have finely tuned roles in cellular signaling and membrane homeostasis. In Bacteria, however, inositol lipid production is rare. Recently, the prominent human gut bacterium Bacteroides thetaiotaomicron (BT) was reported to produce inositol lipids, including inositol sphingolipids, but the pathways remain ambiguous and their prevalence unclear. Here, we investigated the gene cluster responsible for inositol lipid synthesis in BT using a novel strain with inducible control of sphingolipid synthesis. We characterized the biosynthetic pathway from myo-inositol-phosphate (MIP) synthesis to phosphoinositol-dihydroceramide, including structural and kinetic studies of the enzyme MIP synthase (MIPS). We determined the crystal structure of recombinant BT MIPS with bound NAD cofactor at 2.0 Å resolution, and identified the first reported phosphatase for the conversion of bacterially-derived phosphatidylinositol phosphate (PIP) to phosphatidylinositol (PI). Transcriptomic analysis indicated inositol production is nonessential but its loss alters BT capsule expression. Bioinformatic and lipidomic comparisons of Bacteroidetes species revealed a novel second putative pathway for bacterial PI synthesis without a PIP intermediate. Our results indicate that inositol sphingolipid production, via one of the two pathways, is widespread in host-associated Bacteroidetes, and may be implicated in host interactions both indirectly via the capsule and directly through inositol lipid provisioning.

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