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 evolutionarily related to vertebrate lens beta gamma-crystallins. RESULTS: The three-dimensional solution structure of Ca(2+)-loaded protein S has been determined using multi-dimensional heteronuclear NMR spectroscopy. (Sixty structures were calculated, from which thirty were selected with a root mean square difference from the mean of 0.38 A for backbone atoms and 1.22 A for all non-hydrogen atoms.) The structure was analyzed and compared in detail with X-ray crystallographic structures of beta gamma-crystallins. The two internally homologous domains of protein S were compared, and hydrophobic cores, domain interfaces, surface ion pairing, amino-aromatic interactions and potential modes of multimerization are discussed. CONCLUSIONS: Structural features of protein S described here help to explain its overall thermostability, as well as the higher stability and Ca2+ affinity of the amino-terminal domain relative to the carboxy-terminal domain. Two potential modes of multimerization are proposed involving cross-linking of protein S molecules through surface Ca(2+)-binding sites and formation of the intramolecular protein S or gamma B-crystallin interdomain interface in an intermolecular content. This structural analysis may also have implications for Ca(2+)-dependent cell-cell interactions mediated by the vertebrate cadherins and Dictyostelium discoideum protein gp24.
[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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11-24-2010 09:01 PM
[NMR paper] Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as d
Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR.
Related Articles Three-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...
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11-24-2010 08:49 PM
[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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11-19-2010 08:44 PM
[NMR paper] The NMR solution structure of intestinal fatty acid-binding protein complexed with pa
The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: application of a novel distance geometry algorithm.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: application of a novel distance geometry algorithm.
J Mol Biol. 1996 Dec 6;264(3):585-602
Authors: Hodsdon ME, Ponder JW, Cistola DP
The three-dimensional solution structure of rat...
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08-22-2010 02:20 PM
[NMR paper] NMR solution structure of calcium-saturated skeletal muscle troponin C.
NMR solution structure of calcium-saturated skeletal muscle troponin C.
Related Articles NMR solution structure of calcium-saturated skeletal muscle troponin C.
Biochemistry. 1995 Dec 12;34(49):15953-64
Authors: Slupsky CM, Sykes BD
Troponin C (TnC) is an 18 kDa (162-residue) thin-filament calcium-binding protein responsible for triggering muscle contraction upon the release of calcium from the sarcoplasmic reticulum. The structure of TnC with two calcium ions bound has previously been solved by X-ray methods. Shown here is the solution...
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08-22-2010 03:50 AM
[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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08-22-2010 03:33 AM
[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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[NMR paper] Determination of the solution structure of a synthetic two-site calcium-binding homod
Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.
Related Articles Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.
Biochemistry. 1992 Oct 13;31(40):9572-80
Authors: Shaw GS, Hodges RS, Sykes BD
The solution structure of a 34-residue synthetic calcium-binding peptide from site III of chicken troponin-C has been determined by 1H NMR spectroscopy. In solution and in the presence of calcium...
NMR-derived three-dimensional solution structure of protein S complexed with calcium.
Linear Mode
