scholarly journals Solution Structure of 4′-Phosphopantetheine - GmACP3 fromGeobacter metallireducens: A Specialized Acyl Carrier Protein with Atypical Structural Features and a Putative Role in Lipopolysaccharide Biosynthesis

Biochemistry ◽  
2011 ◽  
Vol 50 (9) ◽  
pp. 1442-1453 ◽  
Author(s):  
Theresa A. Ramelot ◽  
Matthew J. Smola ◽  
Hsiau-Wei Lee ◽  
Colleen Ciccosanti ◽  
Keith Hamilton ◽  
...  
Keyword(s):  
Solution Structure ◽  
Acyl Carrier Protein ◽  
Structural Features ◽  
Carrier Protein ◽  
Putative Role ◽  
Lipopolysaccharide Biosynthesis

scholarly journals Novel Structural Components Contribute to the High Thermal Stability of Acyl Carrier Protein from Enterococcus faecalis

2015 ◽  
Vol 291 (4) ◽  
pp. 1692-1702 ◽  
Author(s):  
Young-Guen Park ◽  
Min-Cheol Jung ◽  
Heesang Song ◽  
Ki-Woong Jeong ◽  
Eunjung Bang ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Enterococcus Faecalis ◽  
Solution Structure ◽  
Acyl Carrier Protein ◽  
Acyl Chain ◽  
Structural Features ◽  
High Thermal Stability ◽  
Carrier Protein ◽  
Thermal Stabilities ◽  
Binding Cavity

Enterococcus faecalis is a Gram-positive, commensal bacterium that lives in the gastrointestinal tracts of humans and other mammals. It causes severe infections because of high antibiotic resistance. E. faecalis can endure extremes of temperature and pH. Acyl carrier protein (ACP) is a key element in the biosynthesis of fatty acids responsible for acyl group shuttling and delivery. In this study, to understand the origin of high thermal stabilities of E. faecalis ACP (Ef-ACP), its solution structure was investigated for the first time. CD experiments showed that the melting temperature of Ef-ACP is 78.8 °C, which is much higher than that of Escherichia coli ACP (67.2 °C). The overall structure of Ef-ACP shows the common ACP folding pattern consisting of four α-helices (helix I (residues 3–17), helix II (residues 39–53), helix III (residues 60–64), and helix IV (residues 68–78)) connected by three loops. Unique Ef-ACP structural features include a hydrophobic interaction between Phe45 in helix II and Phe18 in the α1α2 loop and a hydrogen bonding between Ser15 in helix I and Ile20 in the α1α2 loop, resulting in its high thermal stability. Phe45-mediated hydrophobic packing may block acyl chain binding subpocket II entry. Furthermore, Ser58 in the α2α3 loop in Ef-ACP, which usually constitutes a proline in other ACPs, exhibited slow conformational exchanges, resulting in the movement of the helix III outside the structure to accommodate a longer acyl chain in the acyl binding cavity. These results might provide insights into the development of antibiotics against pathogenic drug-resistant E. faecalis strains.

scholarly journals Solution Structure of B. subtilis Acyl Carrier Protein

Structure ◽  
2001 ◽  
Vol 9 (4) ◽  
pp. 277-287 ◽  
Author(s):  
Guang-Yi Xu ◽  
Amy Tam ◽  
Laura Lin ◽  
Jeffrey Hixon ◽  
Christian C. Fritz ◽  
...  
Keyword(s):  
Solution Structure ◽  
Acyl Carrier Protein ◽  
Carrier Protein

Solution Structure of an Acyl Carrier Protein Domain from a Fungal Type I Polyketide Synthase,

Biochemistry ◽  
2010 ◽  
Vol 49 (10) ◽  
pp. 2186-2193 ◽  
Author(s):  
Pakorn Wattana-amorn ◽  
Christopher Williams ◽  
Eliza Płoskoń ◽  
Russell J. Cox ◽  
Thomas J. Simpson ◽  
...  
Keyword(s):  
Solution Structure ◽  
Polyketide Synthase ◽  
Acyl Carrier Protein ◽  
Protein Domain ◽  
Carrier Protein ◽  
Type I

scholarly journals Solution Structure of the Tandem Acyl Carrier Protein Domains from a Polyunsaturated Fatty Acid Synthase Reveals Beads-on-a-String Configuration

PLoS ONE ◽  
2013 ◽  
Vol 8 (2) ◽  
pp. e57859 ◽  
Author(s):  
Uldaeliz Trujillo ◽  
Edwin Vázquez-Rosa ◽  
Delise Oyola-Robles ◽  
Loren J. Stagg ◽  
David A. Vassallo ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Polyunsaturated Fatty Acid ◽  
Solution Structure ◽  
Fatty Acid Synthase ◽  
Acyl Carrier Protein ◽  
Protein Domains ◽  
Carrier Protein

Acyl carrier protein: structure–function relationships in a conserved multifunctional protein family

2007 ◽  
Vol 85 (6) ◽  
pp. 649-662 ◽  
Author(s):  
David M. Byers ◽  
Huansheng Gong
Keyword(s):  
Fatty Acid ◽  
Active Sites ◽  
Fatty Acid Synthase ◽  
Acyl Carrier Protein ◽  
Divalent Cations ◽  
Structural Features ◽  
Carrier Protein ◽  
Type I ◽  
Prosthetic Group

Acyl carrier protein (ACP) is a universal and highly conserved carrier of acyl intermediates during fatty acid synthesis. In yeast and mammals, ACP exists as a separate domain within a large multifunctional fatty acid synthase polyprotein (type I FAS), whereas it is a small monomeric protein in bacteria and plastids (type II FAS). Bacterial ACPs are also acyl donors for synthesis of a variety of products, including endotoxin and acylated homoserine lactones involved in quorum sensing; the distinct and essential nature of these processes in growth and pathogenesis make ACP-dependent enzymes attractive antimicrobial drug targets. Additionally, ACP homologues are key components in the production of secondary metabolites such as polyketides and nonribosomal peptides. Many ACPs exhibit characteristic structural features of natively unfolded proteins in vitro, with a dynamic and flexible conformation dominated by 3 parallel α helices that enclose the thioester-linked acyl group attached to a phosphopantetheine prosthetic group. ACP conformation may also be influenced by divalent cations and interaction with partner enzymes through its “recognition” helix II, properties that are key to its ability to alternately sequester acyl groups and deliver them to the active sites of ACP-dependent enzymes. This review highlights recent progress in defining how the structural features of ACP are related to its multiple carrier roles in fatty acid metabolism.

scholarly journals The genome of a Bacteroidetes inhabitant of the human gut encodes a structurally distinct enoyl-acyl carrier protein reductase (FabI)

2020 ◽  
Vol 295 (22) ◽  
pp. 7635-7652
Author(s):  
Christopher D. Radka ◽  
Matthew W. Frank ◽  
Jiangwei Yao ◽  
Jayaraman Seetharaman ◽  
Darcie J. Miller ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Conformational Change ◽  
Conformational Changes ◽  
Active Site ◽  
Acyl Carrier Protein ◽  
Acid Synthesis ◽  
Binding Pocket ◽  
Structural Features ◽  
Antibacterial Drug ◽  
Carrier Protein

Enoyl-acyl carrier protein reductase (FabI) catalyzes a rate-controlling step in bacterial fatty-acid synthesis and is a target for antibacterial drug development. A phylogenetic analysis shows that FabIs fall into four divergent clades. Members of clades 1–3 have been structurally and biochemically characterized, but the fourth clade, found in members of phylum Bacteroidetes, is uncharacterized. Here, we identified the unique structure and conformational changes that distinguish clade 4 FabIs. Alistipes finegoldii is a prototypical Bacteroidetes inhabitant of the gut microbiome. We found that A. finegoldii FabI (AfFabI) displays cooperative kinetics and uses NADH as a cofactor, and its crystal structure at 1.72 Å resolution showed that it adopts a Rossmann fold as do other characterized FabIs. It also disclosed a carboxyl-terminal extension that forms a helix–helix interaction that links the protomers as a unique feature of AfFabI. An AfFabI·NADH crystal structure at 1.86 Å resolution revealed that this feature undergoes a large conformational change to participate in covering the NADH-binding pocket and establishing the water channels that connect the active site to the central water well. Progressive deletion of these interactions led to catalytically compromised proteins that fail to bind NADH. This unique conformational change imparted a distinct shape to the AfFabI active site that renders it refractory to a FabI drug that targets clade 1 and 3 pathogens. We conclude that the clade 4 FabI, found in the Bacteroidetes inhabitants of the gut, have several structural features and conformational transitions that distinguish them from other bacterial FabIs.

scholarly journals The Solution Structure of Acyl Carrier Protein fromMycobacterium tuberculosis

2002 ◽  
Vol 277 (18) ◽  
pp. 15874-15880 ◽  
Author(s):  
Hing C. Wong ◽  
Gaohua Liu ◽  
Yong-Mei Zhang ◽  
Charles O. Rock ◽  
Jie Zheng
Keyword(s):  
Solution Structure ◽  
Acyl Carrier Protein ◽  
Carrier Protein

scholarly journals Solution structure of Asl1650, an acyl carrier protein fromAnabaenasp. PCC 7120 with a variant phosphopantetheinylation-site sequence

2006 ◽  
Vol 15 (5) ◽  
pp. 1030-1041 ◽  
Author(s):  
Margaret A. Johnson ◽  
Wolfgang Peti ◽  
Torsten Herrmann ◽  
Ian A. Wilson ◽  
Kurt Wüthrich
Keyword(s):  
Solution Structure ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Pcc 7120

NMR: pseudoenergy approach to the solution structure of acyl carrier protein

Biochemistry ◽  
1987 ◽  
Vol 26 (15) ◽  
pp. 4652-4660 ◽  
Author(s):  
T. A. Holak ◽  
J. H. Prestegard ◽  
J. D. Forman
Keyword(s):  
Solution Structure ◽  
Acyl Carrier Protein ◽  
Carrier Protein
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