Ubiquitin specific protease 7 (USP7) is a deubiquitinating enzyme, which removes ubiquitin tag from numerous protein substrates involved in diverse cellular processes such as cell cycle regulation, apoptosis and DNA damage response. USP7 affects stability, interaction network and cellular localization of its cellular and viral substrates by controlling their ubiquitination status. The large 41 kDa catalytic domain of USP7 harbors the active site of the enzyme. Here we present a nearly complete...
[NMR paper] Unambiguous Side-Chain Assignments for Solid-State NMR Structure Elucidation of Nondeuterated Proteins via a Combined 5D/4D Side-Chain-to-Backbone Experiment
Unambiguous Side-Chain Assignments for Solid-State NMR Structure Elucidation of Nondeuterated Proteins via a Combined 5D/4D Side-Chain-to-Backbone Experiment
Owing to fast-magic-angle-spinning technology, proton-detected solid-state NMR has been facilitating the analysis of insoluble, crystalline, sedimented, and membrane proteins. However, potential applications have been largely restricted by limited access to side-chain resonances. The recent availability of spinning frequencies exceeding 100 kHz in principle now allows direct probing of all protons without the need for partial...
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[NMR paper] Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Related Articles Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Biomol NMR Assign. 2014 Feb 4;
Authors: Jean NL, Bougault C, Derouaux A, Callens G, Vollmer W, Simorre JP
Abstract
The peptidoglycan is a major component of the bacterial cell wall and is essential to maintain cellular integrity and cell shape. Penicillin-Binding Proteins (PBPs) catalyze the final...
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02-05-2014 06:08 PM
[NMR paper] Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Related Articles Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Biomol NMR Assign. 2013 Dec 24;
Authors: Peterson TA, Yu L, Piper RC
Abstract
Vps28 is one of four cytosolic proteins comprising the endosomal sorting complex required for transport I (ESCRT-I). ESCRT-I is involved in sorting ubiquitinated proteins to multivesicular bodies as well as in mediating budding of retroviruses. Here, we report the backbone...
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12-25-2013 03:39 PM
[NMR paper] Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.
Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.
Related Articles Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.
Biomol NMR Assign. 2013 Dec 24;
Authors: Castellen P, Sforça ML, Gueiros-Filho FJ, de Mattos Zeri AC
Abstract
Bacterial cell division proteins must assemble at the middle of the cell to ensure the viability of both daughter cells. The first step in the assembly of the...
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[NMR paper] (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Related Articles (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Biomol NMR Assign. 2013 May 18;
Authors: Fonner BA, Tripet BP, Lui M, Zhu H, Lei B, Copié V
Abstract
Staphylococcus aureus is an opportunistic pathogen that...
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05-21-2013 02:34 PM
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Biomol NMR Assign. 2011 Jun 7;
Authors: Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we...
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06-08-2011 11:30 AM
[NMR paper] Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic t
Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
Related Articles Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
J Biomol NMR. 2005 Apr;31(4):279-93
Authors: Gammeren AJ, Hulsbergen FB, Hollander JG, Groot HJ
This study reports the sequence specific chemical shifts...
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[NMR paper] Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts
Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Related Articles Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Protein Sci. 2003 Sep;12(9):2104-8
Authors: Liu W, Rumbley J, Englander SW, Wand AJ
The mutant of horse heart cytochrome c was expressed in E. coli during growth on isotopically enriched minimal media. Complete resonance assignments of both the diamagnetic reduced (spin zero) and paramagnetic oxidized (spin (1/2))...