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10.1107/S1399004715016429 http://scihub22266oqcxt.onion/10.1107/S1399004715016429 26527143/?report=reader!4631478!26527143     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Acta+Crystallogr+D+Biol+Crystallogr 2015 ; 71 (Pt 11): 2267-77 Nephropedia Template TP {{tp|p=26527143|t=2015. Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3 )(9) adenyltransferase |pdf=|usr=}}{{26527143}} gab.com Text Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3 )(9) adenyltransferase JO: Acta Crystallogr D Biol Crystallogr http://www.kidney.de/pget.php?&tw=1&pmid=26527143 #FOAvip Aminoglycoside resistance is commonly conferred by enzymatic modification of drugs by aminoglycoside-modifying enzymes such as aminoglycoside nucleotidyltransferases (ANTs). Here, the first crystal structure of an ANT(3'')(9) adenyltransferase, AadA from Salmonella enterica, is presented. AadA catalyses the magnesium-dependent transfer of adenosine monophosphate from ATP to the two chemically dissimilar drugs streptomycin and spectinomycin. The structure was solved using selenium SAD phasing and refined to 2.5 A resolution. AadA consists of a nucleotidyltransferase domain and an alpha-helical bundle domain. AadA crystallizes as a monomer and is a monomer in solution as confirmed by small-angle X-ray scattering, in contrast to structurally similar homodimeric adenylating enzymes such as kanamycin nucleotidyltransferase. Isothermal titration calorimetry experiments show that ATP binding has to occur before binding of the aminoglycoside substrate, and structure analysis suggests that ATP binding repositions the two domains for aminoglycoside binding in the interdomain cleft. Candidate residues for ligand binding and catalysis were subjected to site-directed mutagenesis. In vivo resistance and in vitro binding assays support the role of Glu87 as the catalytic base in adenylation, while Arg192 and Lys205 are shown to be critical for ATP binding. Twit Text FOAVip Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3 )(9) adenyltransferase ????Acta Crystallogr D Biol Crystallogr http://www.kidney.de/pget.php?&tw=1&pmid=26527143 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26527143 #FOAvip English Wikipedia <ref>{{Cite pmid|26527143}}</ref> Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3 )(9) adenyltransferase #MMPMID26527143 Chen Y; Nasvall J; Wu S; Andersson DI; Selmer M Acta Crystallogr D Biol Crystallogr 2015[Nov]; 71 (Pt 11): 2267-77 PMID26527143show ga Aminoglycoside resistance is commonly conferred by enzymatic modification of drugs by aminoglycoside-modifying enzymes such as aminoglycoside nucleotidyltransferases (ANTs). Here, the first crystal structure of an ANT(3'')(9) adenyltransferase, AadA from Salmonella enterica, is presented. AadA catalyses the magnesium-dependent transfer of adenosine monophosphate from ATP to the two chemically dissimilar drugs streptomycin and spectinomycin. The structure was solved using selenium SAD phasing and refined to 2.5 A resolution. AadA consists of a nucleotidyltransferase domain and an alpha-helical bundle domain. AadA crystallizes as a monomer and is a monomer in solution as confirmed by small-angle X-ray scattering, in contrast to structurally similar homodimeric adenylating enzymes such as kanamycin nucleotidyltransferase. Isothermal titration calorimetry experiments show that ATP binding has to occur before binding of the aminoglycoside substrate, and structure analysis suggests that ATP binding repositions the two domains for aminoglycoside binding in the interdomain cleft. Candidate residues for ligand binding and catalysis were subjected to site-directed mutagenesis. In vivo resistance and in vitro binding assays support the role of Glu87 as the catalytic base in adenylation, while Arg192 and Lys205 are shown to be critical for ATP binding. |Adenosine Triphosphate/metabolism[MESH] |Amino Acid Sequence[MESH] |Crystallography, X-Ray[MESH] |Models, Molecular[MESH] |Molecular Sequence Data[MESH] |Nucleotidyltransferases/*chemistry/metabolism[MESH] |Protein Conformation[MESH] |Salmonella enterica/*chemistry/*enzymology/metabolism[MESH]Structure of AadA from Salmonella enterica: a monomeric aminoglycoside(epmc).pdf DeepDyve Pubget Overpricing