Related ArticlesThree-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR.
Biochemistry. 2002 Jan 22;41(3):788-96
Authors: Rustandi RR, Baldisseri DM, Inman KG, Nizner P, Hamilton SM, Landar A, Landar A, Zimmer DB, Weber DJ
S100A1, a member of the S100 protein family, is an EF-hand containing Ca(2+)-binding protein (93 residues per subunit) with noncovalent interactions at its dimer interface. Each subunit of S100A1 has four alpha-helices and a small antiparallel beta-sheet consistent with two helix-loop-helix calcium-binding domains [Baldiserri et al. (1999) J. Biomol. NMR 14, 87-88]. In this study, the three-dimensional structure of reduced apo-S100A1 was determined by NMR spectroscopy using a total of 2220 NOE distance constraints, 258 dihedral angle constraints, and 168 backbone hydrogen bond constraints derived from a series of 2D, 3D, and 4D NMR experiments. The final structure was found to be globular and compact with the four helices in each subunit aligning to form a unicornate-type four-helix bundle. Intermolecular NOE correlations were observed between residues in helices 1 and 4 from one subunit to residues in helices 1' and 4' of the other subunit, respectively, consistent with the antiparallel alignment of the two subunits to form a symmetric X-type four-helix bundle as found for other members of the S100 protein family. Because of the similarity of the S100A1 dimer interface to that found for S100B, it was possible to calculate a model of the S100A1/B heterodimer. This model is consistent with a number of NMR chemical shift changes observed when S100A1 is titrated into a sample of (15)N-labeled S100B. Helix 3 (and 3') of S100A1 was found to have an interhelical angle of -150 degrees with helix 4 (and 4') in the apo state. This crossing angle is quite different (>50 degrees ) from that typically found in other EF-hand containing proteins such as apocalmodulin and apotroponin C but more similar to apo-S100B, which has an interhelical angle of -166 degrees. As with S100B, it is likely that the second EF-hand of apo-S100A1 reorients dramatically upon the addition of Ca(2+), which can explain the Ca(2+) dependence that S100A1 has for binding several of its biological targets.
Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
J Struct Biol. 2011 Feb 2;
Authors: Nowakowski M, Jaremko L, Jaremko M, Zhukov I, Belczyk A, Bierzy?ski A, Ejchart A
S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits. S100A1, like most...
[NMR paper] NMR solution structure of calerythrin, an EF-hand calcium-binding protein from Saccha
NMR solution structure of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea.
Related Articles NMR solution structure of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea.
Eur J Biochem. 2003 Jun;270(11):2505-12
Authors: Tossavainen H, Permi P, Annila A, Kilpeläinen I, Drakenberg T
The structure of calerythrin, a prokaryotic 20 kDa calcium-binding protein has been determined by solution NMR spectroscopy. Distance, dihedral angle, J coupling, secondary chemical shift, residual dipolar...
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[NMR paper] NMR derived solution structure of an EF-hand calcium-binding protein from Entamoeba H
NMR derived solution structure of an EF-hand calcium-binding protein from Entamoeba Histolytica.
Related Articles NMR derived solution structure of an EF-hand calcium-binding protein from Entamoeba Histolytica.
Biochemistry. 2001 Dec 4;40(48):14392-403
Authors: Atreya HS, Sahu SC, Bhattacharya A, Chary KV, Govil G
We present the three-dimensional (3D) solution structure of a calcium-binding protein from Entamoeba histolytica (EhCaBP), an etiologic agent of amoebiasis affecting millions worldwide. EhCaBP is a 14.7 kDa (134 residues) monomeric...
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[NMR paper] Backbone dynamics of the calcium-signaling protein apo-S100B as determined by 15N NMR
Backbone dynamics of the calcium-signaling protein apo-S100B as determined by 15N NMR relaxation.
Related Articles Backbone dynamics of the calcium-signaling protein apo-S100B as determined by 15N NMR relaxation.
Biochemistry. 2001 Mar 27;40(12):3439-48
Authors: Inman KG, Baldisseri DM, Miller KE, Weber DJ
Backbone dynamics of homodimeric apo-S100B were studied by (15)N nuclear magnetic resonance relaxation at 9.4 and 14.1 T. Longitudinal relaxation (T(1)), transverse relaxation (T(2)), and the (15)N- NOE were measured for 80 of 91 backbone...
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[NMR paper] NMR-derived three-dimensional solution structure of protein S complexed with calcium.
NMR-derived three-dimensional solution structure of protein S complexed with calcium.
Related Articles NMR-derived three-dimensional solution structure of protein S complexed with calcium.
Structure. 1994 Feb 15;2(2):107-22
Authors: Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M
BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is...
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[NMR paper] NMR-derived three-dimensional solution structure of protein S complexed with calcium.
NMR-derived three-dimensional solution structure of protein S complexed with calcium.
Related Articles NMR-derived three-dimensional solution structure of protein S complexed with calcium.
Structure. 1994 Feb 15;2(2):107-22
Authors: Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M
BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is...
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[NMR paper] Three-dimensional structure in solution of a wheat lipid-transfer protein from multid
Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers.
Eur J Biochem. 1994 Dec 1;226(2):413-22
Authors: Gincel E, Simorre JP, Caille A, Marion D, Ptak M, Vovelle F
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