Related ArticlesNMR Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.
Biochemistry. 2016 May 10;
Authors: Byeon IL, Byeon CH, Wu T, Mitra M, Singer D, Levin JG, Gronenborn AM
Abstract
Human APOBEC3B (A3B) is a member of the APOBEC3 (A3) family of cytidine deaminases, which function as DNA mutators and restrict viral pathogens and endogenous retrotransposons. Recently, A3B was identified as a major source of genetic heterogeneity in several human cancers. Here, we determined the solution NMR structure of the catalytically active C-terminal domain (CTD) of A3B and performed detailed analyses of its deaminase activity. The core of the structure comprises a central five-stranded ?-sheet with six surrounding helices, common to all A3 proteins. The structural fold is most similar to that of A3A and A3G-CTD, with the most prominent difference found in loop 1. The catalytic activity of A3B-CTD is ~15-fold less than that of A3A, although both exhibit similar pH dependence. Interestingly, A3B-CTD with an A3A loop 1 substitution had significantly increased deaminase activity, while a single residue change (H29R) in A3A loop 1 reduced A3A activity to the level seen with A3B-CTD. This establishes that loop 1 plays an important role in A3-catalyzed deamination by precisely positioning the deamination-targeted C into the active site. Overall, our data provide important insights into the determinants for the activities of individual A3 proteins and facilitate understanding of their biological function.
PMID: 27163633 [PubMed - as supplied by publisher]
[NMR paper] Structural basis of a temporin 1b analogue antimicrobial activity against Gram negative bacteria determined by CD and NMR techniques in cellular environment.
Structural basis of a temporin 1b analogue antimicrobial activity against Gram negative bacteria determined by CD and NMR techniques in cellular environment.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Structural basis of a temporin 1b analogue antimicrobial activity against Gram negative bacteria determined by CD and NMR techniques in cellular environment.
ACS Chem Biol. 2015 Apr 17;10(4):965-9
Authors: Malgieri G, Avitabile C, Palmieri M, D'Andrea LD, Isernia C,...
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[NMR paper] NMR Structure and Dynamics of the Resuscitation Promoting Factor RpfC Catalytic Domain.
NMR Structure and Dynamics of the Resuscitation Promoting Factor RpfC Catalytic Domain.
Related Articles NMR Structure and Dynamics of the Resuscitation Promoting Factor RpfC Catalytic Domain.
PLoS One. 2015;10(11):e0142807
Authors: Maione V, Ruggiero A, Russo L, De Simone A, Pedone PV, Malgieri G, Berisio R, Isernia C
Abstract
Mycobacterium tuberculosis latent infection is maintained for years with no clinical symptoms and no adverse effects for the host. The mechanism through which dormant M. tuberculosis resuscitates and...
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11-19-2015 04:08 AM
[NMR paper] NMR study of the Z-DNA binding mode and B-Z transition activity of the Z? domain of human ADAR1 when perturbed by mutation on the ?3 helix and ?-hairpin.
NMR study of the Z-DNA binding mode and B-Z transition activity of the Z? domain of human ADAR1 when perturbed by mutation on the ?3 helix and ?-hairpin.
Related Articles NMR study of the Z-DNA binding mode and B-Z transition activity of the Z? domain of human ADAR1 when perturbed by mutation on the ?3 helix and ?-hairpin.
Arch Biochem Biophys. 2014 Jul 7;
Authors: Jeong M, Lee AR, Kim HE, Choi YG, Choi BS, Lee JH
Abstract
The Z? domains of human ADAR1 (Z?ADAR1) bind to Z-DNA via interaction mediated by the ?3-core and ?-hairpin....
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07-12-2014 04:28 AM
[NMR paper] Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
Related Articles Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
J Struct Biol. 2013 Nov 6;
Authors: Jaremko M, Jaremko L, Nowakowski M, Wojciechowski M, Szczepanowski RH, Panecka R, Zhukov I, Bochtler M, Ejchart A
Abstract
We report a high resolution NMR structure and (15)N relaxation studies of the first catalytic cysteine half-domain (FCCH) of the mouse ubiquitin-activating enzyme E1, together with...
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[NMR paper] Relation of enzyme activity to local/global stability of murine adenosine deaminase:
Relation of enzyme activity to local/global stability of murine adenosine deaminase: 19F NMR studies.
Related Articles Relation of enzyme activity to local/global stability of murine adenosine deaminase: 19F NMR studies.
J Mol Biol. 2005 Jan 21;345(3):599-610
Authors: Shu Q, Frieden C
Adenosine deaminase (ADA, EC 3.5.4.4) is a ubiquitous (beta/alpha)8-barrel enzyme crucial for purine metabolism and normal immune competence. In this study, it was observed that loss of enzyme activity of murine ADA (mADA) precedes the global secondary and...
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11-24-2010 11:14 PM
[NMR paper] Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with w
Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Related Articles Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Biochemistry. 2003 Sep 30;42(38):11100-8
Authors: Cai S, Stevens SY, Budor AP, Zuiderweg ER
The interaction of solvent of the substrate binding domain of the bacterial heat shock 70 chaperone protein DnaK was studied in its apo form and with bound hydrophobic substrate peptide, using refined nuclear magnetic...
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[NMR paper] NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain:
NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Related Articles NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Biochemistry. 1998 Jun 2;37(22):7929-40
Authors: Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER
The solution structure of the 21 kDa substrate-binding domain of the Escherichia coli Hsp70-chaperone protein DnaK (DnaK 386-561) has been determined to a precision...
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11-17-2010 11:06 PM
[NMR paper] Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spec
Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity.
Related Articles Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity.
Biochemistry. 1995 Nov 21;34(46):15351-8
Authors: Boerner RJ, Consler TG, Gampe RT, Weigl D, Willard DH, Davis DG, Edison AM, Loganzo F, Kassel DB, Xu RX
During solution...