The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence identity with any member of this enzyme family, the residues involved in substrate-recognition and catalysis are highly conserved in NP_344798.1. NMR studies showed binding affinity of NP_344798.1 for nucleotides and revealed ?s to ms time scale rate processes involving residues constituting the active site. The results thus obtained indicate that large-amplitude rearrangements of regular secondary structures facilitate the penetration of the substrate into the occluded nucleotide-binding site of NP_344798.1 and, by inference based on sequence and structural homology, probably a wide range of other nucleotide-adding enzymes.
[NMR paper] NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
Related Articles NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.
Protein Sci. 2016 Jan 8;
Authors: Mohanty B, Geralt M, Wüthrich K, Serrano P
Abstract
The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence...
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NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
Abstract
The protein NP_344798.1 from Streptococcus pneumoniae TIGR4 exhibits a head and base-interacting neck domain architecture, as observed in class II nucleotide-adding enzymes. Although it has less than 20% overall sequence identity with any member of this enzyme family, the residues involved in substrate-recognition and catalysis are highly conserved in NP_344798.1. NMR studies showed binding affinity of NP_344798.1 for nucleotides and revealed ?s to ms time scale rate processes...
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01-09-2016 04:06 PM
[NMR paper] NMR-based structural analysis of threonylcarbamoyl-AMP synthase and its substrate interactions.
NMR-based structural analysis of threonylcarbamoyl-AMP synthase and its substrate interactions.
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J Biol Chem. 2015 Jun 9;
Authors: Harris KA, Bobay BG, Sarachan KL, Sims AF, Bilbille Y, Deutsch C, Iwata-Reuyl D, Agris PF
Abstract
The hypermodified nucleoside N(6)-threonylcarbamoyladenosine (t(6)A37) is present in many distinct tRNA species and has been found in organisms in all domains of life. This...
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[NMR paper] NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.
NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.
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Nat Commun. 2013;4:1890
Authors: Byeon IJ, Ahn J, Mitra M, Byeon CH, Hercík K, Hritz J, Charlton LM, Levin JG, Gronenborn AM
Abstract
Human APOBEC3A is a single-stranded DNA cytidine deaminase that restricts viral pathogens and endogenous retrotransposons, and has a role in the innate immune response. Furthermore, its...
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[NMR paper] NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus t
NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism.
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J Biol Chem. 2004 Aug 6;279(32):33958-67
Authors: Revington M, Holder TM, Zuiderweg ER
We present an NMR investigation of the nucleotide-dependent conformational properties of a 44-kDa nucleotide binding...
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[NMR paper] Investigating structural changes in the lipid bilayer upon insertion of the transmemb
Investigating structural changes in the lipid bilayer upon insertion of the transmembrane domain of the membrane-bound protein phospholamban utilizing 31P and 2H solid-state NMR spectroscopy.
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Biophys J. 2004 Mar;86(3):1564-73
Authors: Dave PC, Tiburu EK, Damodaran K, Lorigan GA
Phospholamban (PLB) is a 52-amino acid integral membrane...
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[NMR paper] Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon
Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein.
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Int J Biol Macromol. 2003 Dec;33(4-5):193-201
Authors: Cicero DO, Melino S, Orsale M, Brancato G, Amadei A,...
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[NMR paper] Proton NMR and structural features of a 24-nucleotide RNA hairpin.
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Biochemistry. 1995 May 16;34(19):6488-503
Authors: Borer PN, Lin Y, Wang S, Roggenbuck MW, Gott JM, Uhlenbeck OC, Pelczer I
The three-dimensional conformation of a 24-nucleotide variant of the RNA binding sequence for the coat protein of bacteriophage R17 has been analyzed using NMR, molecular dynamics, and energy minimization. The imino proton spectrum is consistent with base pairing...
NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes
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