[NMR paper] (1)H, (13)C and (15)N NMR assignments of a bacterial immunoglobulin-like domain (group 2) of a protein of a bacterium Paenarthrobacter aurescens TC1.
Related Articles(1)H, (13)C and (15)N NMR assignments of a bacterial immunoglobulin-like domain (group 2) of a protein of a bacterium Paenarthrobacter aurescens TC1.
Abstract
The bacterial immunoglobulin-like (Big) domain is one of the prevalent domain types, which facilitates cell-cell adhesion by assembling into multi-domain architectures. We selected a four Big_2 domain protein (named 'Arig') from a Gram positive, Paenarthrobacter aurescens TC1 (known earlier as Arthrobacter aurescens TC1). In an attempt to characterize structural and ligand-binding features of individual Big_2 domains, we have cloned, overexpressed, isolated and purified the second Big_2 domain of Arig along with a few of its adjacent Big_2 domain residues (residue 143 to 269) referred to as 'Arig2'. The (13)C/(15)N-doubly-labeled His-tagged Arig2 (133 residues long) showed an ordered conformation as revealed by the well dispersed 2D [(15)N-(1)H]-HSQC spectrum. Subsequently, a suite of heteronuclear 3D NMR experiments has enabled almost complete (1)H, (13)C and (15)N NMR resonance assignments of Arig2.
PMID: 28593559 [PubMed - as supplied by publisher]
[NMR paper] NMR solution structure of the terminal immunoglobulin-like domain from the Leptospira host-interacting outer membrane protein, LigB.
NMR solution structure of the terminal immunoglobulin-like domain from the Leptospira host-interacting outer membrane protein, LigB.
Related Articles NMR solution structure of the terminal immunoglobulin-like domain from the Leptospira host-interacting outer membrane protein, LigB.
Biochemistry. 2014 Jul 28;
Authors: Ptak CP, Hsieh CL, Lin YP, Maltsev AS, Raman R, Sharma Y, Oswald RE, Chang YF
Abstract
A number of surface proteins specific to pathogenic strains of Leptospira have been identified. The Lig protein family has shown...
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Structure of bacterial nanowire protein Pilin Modelhints at secrets of conduction - domain-B
Structure of bacterial nanowire protein Pilin Modelhints at secrets of conduction - domain-B
http://www.bionmr.com//t0.gstatic.com/images?q=tbn:ANd9GcSCn6Z34RNX9hqQD01iRxFbqXmTRQat0Mxwx6IJ9O4v98NpOR01IY2UBUd7UTj9hw38lQPTYA
domain-B
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Structure of bacterial nanowire protein Pilin Modelhints at secrets of conduction
domain-B
But the protein by itself isn't enough to reveal how conduction works. Many pilin proteins work together to form a fiber, and Reardon and Mueller only had one. Nor did the researchers have the whole fibre to put into the NMR...
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11-16-2013 03:14 PM
[NMR paper] Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
Related Articles Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
J Am Chem Soc. 2005 Sep 7;127(35):12291-305
Authors: Franks WT, Zhou DH, Wylie BJ, Money BG, Graesser DT, Frericks HL, Sahota G, Rienstra CM
Magic-angle spinning...
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12-01-2010 06:56 PM
[NMR paper] Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium
Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.
Related Articles Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.
Eur J Biochem. 2001 May;268(9):2527-39
Authors: Kremer W, Schuler B, Harrieder S, Geyer M, Gronwald W, Welker C, Jaenicke R, Kalbitzer HR
Cold-shock proteins (Csps) are a subgroup of the cold-induced proteins preferentially expressed in bacteria and other organisms on reduction of the growth temperature below the...
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[NMR paper] Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal prote
Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR.
Related Articles Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR.
Biochemistry. 1994 Apr 19;33(15):4721-9
Authors: Gallagher T, Alexander P, Bryan P, Gilliland GL
The structure of the 56-residue B1 immunoglobulin-binding domain from streptococcal protein G has been determined in two different crystal forms. The crystal structures were deduced by molecular...
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08-22-2010 03:33 AM
[NMR paper] Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal prote
Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR.
Related Articles Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR.
Biochemistry. 1994 Apr 19;33(15):4721-9
Authors: Gallagher T, Alexander P, Bryan P, Gilliland GL
The structure of the 56-residue B1 immunoglobulin-binding domain from streptococcal protein G has been determined in two different crystal forms. The crystal structures were deduced by molecular...
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08-22-2010 03:33 AM
[NMR paper] 1.67-A X-ray structure of the B2 immunoglobulin-binding domain of streptococcal prote
1.67-A X-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain.
Related Articles 1.67-A X-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain.
Biochemistry. 1992 Nov 3;31(43):10449-57
Authors: Achari A, Hale SP, Howard AJ, Clore GM, Gronenborn AM, Hardman KD, Whitlow M
The structure of the B2 immunoglobulin-binding domain of streptococcal protein G has been determined at 1.67-A...
(1)H, (13)C and (15)N NMR assignments of a bacterial immunoglobulin-like domain (group 2) of a protein of a bacterium Paenarthrobacter aurescens TC1.
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