The ring-shaped E. coli ?-clamp protein is an 81 kDa head-to-tail homodimer, which serves as a processivity factor anchoring the replicative polymerase to DNA, thereby increasing replication processivity and speed. In addition, it facilitates numerous protein transactions that take place on DNA during replication, repair, and damage response. We used a structure-based approach to obtain nearly complete Ile, Leu and Val side-chain methyl NMR resonance assignments of the wild-type ?-clamp and its...
[NMR paper] NMR resonance assignments for the nucleotide binding domains of the E. coli clamp loader complex gamma subunit
NMR resonance assignments for the nucleotide binding domains of the E. coli clamp loader complex gamma subunit
The E. coli ? clamp loader is a pentameric complex of ?, ?' and three ? subunits that opens and loads ?-clamp proteins onto DNA in an ATP-dependent process essential for efficient DNA replication. ATP binding to the ? subunits promotes conformational changes that enable the clamp loader to bind and open the ring-shaped ?-clamp homodimer. Here we report the nearly complete backbone and side-chain ¹H, ^(13)C and ^(15)N NMR resonance assignments of the 242-residue truncated ? subunit...
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03-24-2021 11:20 PM
[NMR paper] Backbone-independent NMR resonance assignments of methyl probes in large proteins.
Backbone-independent NMR resonance assignments of methyl probes in large proteins.
Related Articles Backbone-independent NMR resonance assignments of methyl probes in large proteins.
Nat Commun. 2021 Jan 29;12(1):691
Authors: Nerli S, De Paula VS, McShan AC, Sgourakis NG
Abstract
Methyl-specific isotope labeling is a powerful tool to study the structure, dynamics and interactions of large proteins and protein complexes by solution-state NMR. However, widespread applications of this methodology have been limited by challenges in...
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01-31-2021 02:47 PM
[NMR paper] NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine.
NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine.
Related Articles NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine.
J Biomol NMR. 2017 Jun 26;:
Authors: Pederson K, Chalmers GR, Gao Q, Elnatan D, Ramelot TA, Ma LC, Montelione GT, Kennedy MA, Agard DA, Prestegard JH
Abstract
A strategy for acquiring structural information from sparsely isotopically labeled large proteins is illustrated with an application to the E. coli heat-shock...
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06-28-2017 07:37 PM
[NMR paper] NMR resonance assignments for the N-terminal domain of the ? subunit of the E. coli ? clamp loader complex.
NMR resonance assignments for the N-terminal domain of the ? subunit of the E. coli ? clamp loader complex.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR resonance assignments for the N-terminal domain of the ? subunit of the E. coli ? clamp loader complex.
Biomol NMR Assign. 2017 Mar 06;:
Authors: Alyami EM, Rizzo AA, Beuning PJ, Korzhnev DM
Abstract
The ?-clamp protein and the ? clamp loader complex are essential...
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03-09-2017 12:11 AM
3D-TROSY-based backbone and ILV-methyl resonance assignments of a 319-residue homodimer from a single protein sample
3D-TROSY-based backbone and ILV-methyl resonance assignments of a 319-residue homodimer from a single protein sample
Abstract The feasibility of practically complete backbone and ILV methyl chemical shift assignments from a single -labeled protein sample of the truncated form of ligand-free Bst-Tyrosyl tRNA Synthetase (Bst-Î?YRS), a 319-residue predominantly helical homodimer, is established. Protonation of ILV residues at methyl positions does not appreciably detract from the quality of TROSY triple resonance data. The assignments are performed at 40 °C to improve the sensitivity of...
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09-10-2012 01:48 AM
[NMR paper] Resonance assignments and secondary structure analysis of E. coli thioredoxin by magic angle spinning solid-state NMR spectroscopy.
Resonance assignments and secondary structure analysis of E. coli thioredoxin by magic angle spinning solid-state NMR spectroscopy.
Related Articles Resonance assignments and secondary structure analysis of E. coli thioredoxin by magic angle spinning solid-state NMR spectroscopy.
J Phys Chem B. 2005 Sep 29;109(38):18135-45
Authors: Marulanda D, Tasayco ML, Cataldi M, Arriaran V, Polenova T
De novo site-specific 13C and 15N backbone and sidechain resonance assignments are presented for uniformly enriched E. coli thioredoxin, established using...
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12-01-2010 06:56 PM
High-resolution methyl edited GFT NMR experiments for protein resonance assignments a
High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination
Abstract Three-dimensional (3D) structure determination of proteins is benefitted by long-range distance constraints comprising the methyl groups, which constitute the hydrophobic core of proteins. However, in methyl groups (of Ala, Ile, Leu, Met, Thr and Val) there is a significant overlap of 13C and 1H chemical shifts. Such overlap can be resolved using the recently proposed (3,2)D HCCH-COSY, a G-matrix Fourier transform (GFT) NMR based experiment, which facilitates editing...
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09-18-2010 04:53 AM
High-resolution methyl edited GFT NMR experiments for protein resonance assignments a
High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination.
Related Articles High-resolution methyl edited GFT NMR experiments for protein resonance assignments and structure determination.
J Biomol NMR. 2010 Sep 14;
Authors: Jaipuria G, Thakur A, D'Silva P, Atreya HS
Three-dimensional (3D) structure determination of proteins is benefitted by long-range distance constraints comprising the methyl groups, which constitute the hydrophobic core of proteins. However, in methyl groups (of Ala, Ile,...
ILV methyl NMR resonance assignments of the 81*kDa E. coli ?-clamp
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