Abstract
Nearly complete resonance assignment and the high-resolution NMR structure of the acyl-carrier protein from Borrelia burgdorferi, a target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure-determination pipeline, are reported. This protein was chosen as a potential target for drug-discovery efforts because of its involvement in fatty-acid biosynthesis, an essential metabolic pathway, in bacteria. It was possible to assign >98% of backbone resonances and >92% of side-chain resonances using multidimensional NMR spectroscopy. The NMR structure was determined to a backbone r.m.s.d. of 0.4 Å and contained four ?-helices and two 3(10)-helices. A structure-homology search revealed that this protein is highly similar to the acyl-carrier protein from Aquifex aeolicus.
[NMR paper] NMR structure of the sterol carrier protein-2: implications for the biological role.
NMR structure of the sterol carrier protein-2: implications for the biological role.
Related Articles NMR structure of the sterol carrier protein-2: implications for the biological role.
J Mol Biol. 2000 Jan 21;295(3):595-603
Authors: García FL, Szyperski T, Dyer JH, Choinowski T, Seedorf U, Hauser H, Wüthrich K
The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone (15)N spin relaxation parameters and NMR studies of nitroxide spin-labeled substrate binding are presented as a new basis for...
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[NMR paper] Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid
Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid binding sites.
Related Articles Holo-sterol carrier protein-2. (13)C NMR investigation of cholesterol and fatty acid binding sites.
J Biol Chem. 1999 Dec 10;274(50):35425-33
Authors: Stolowich N, Frolov A, Petrescu AD, Scott AI, Billheimer JT, Schroeder F
Although sterol carrier protein-2 (SCP-2) stimulates sterol transfer in vitro, almost nothing is known regarding the identity of the putative cholesterol binding site. Furthermore, the interrelationship(s)...
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[NMR paper] NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer
NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.
Related Articles NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.
J Biomol NMR. 1998 May;11(4):407-14
Authors: Pham TN, Koide S
The crystal structure of outer surface protein A (OspA) from Borrelia burgdorferi contains a single-layer beta-sheet connecting the N- and C-terminal globular domains. The central beta-sheet consists largely of polar amino acids and it is solvent-exposed on both faces, which...
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11-17-2010 11:06 PM
NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermo
NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.
Related Articles NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.
J Struct Funct Genomics. 2010 Oct 5;
Authors: Goroncy AK, Murayama K, Shirouzu M, Kuramitsu S, Kigawa T, Yokoyama S
Sterol carrier protein 2 (SCP-2), also known as nonspecific lipid transfer protein, is a ubiquitous intracellular ~13*kDa protein found in mammals, insects, plants,...
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[NMR paper] The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and
The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination.
Biochemistry. 1997 Feb 18;36(7):1719-29
Authors: Stolowich NJ, Frolov A, Atshaves B, Murphy EJ, Jolly CA, Billheimer JT, Scott AI, Schroeder F
The interaction and orientation of fatty acids...
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08-22-2010 03:31 PM
[NMR paper] The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and
The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The sterol carrier protein-2 fatty acid binding site: an NMR, circular dichroic, and fluorescence spectroscopic determination.
Biochemistry. 1997 Feb 18;36(7):1719-29
Authors: Stolowich NJ, Frolov A, Atshaves B, Murphy EJ, Jolly CA, Billheimer JT, Scott AI, Schroeder F
The interaction and orientation of fatty acids...
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08-22-2010 03:03 PM
[NMR paper] The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver:
The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy.
Related Articles The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy.
J Biomol NMR. 1993 May;3(3):271-84
Authors: Andersen KV, Poulsen FM
The 3D structure of bovine recombinant acyl-coenzyme A binding protein has been determined using multidimensional heteronuclear magnetic...
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[NMR paper] Refinement of the NMR structures for acyl carrier protein with scalar coupling data.
Refinement of the NMR structures for acyl carrier protein with scalar coupling data.
Related Articles Refinement of the NMR structures for acyl carrier protein with scalar coupling data.
Proteins. 1990;8(4):377-85
Authors: Kim Y, Prestegard JH
Structure determination of small proteins using NMR data is most commonly pursued by combining NOE derived distance constraints with inherent constraints based on chemical bonding. Ideally, one would make use of a variety of experimental observations, not just distance constraints. Here, coupling...
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
Linear Mode
