Crystal structure of the MazG-related nucleoside triphosphate pyrophosphohydrolase from Thermotoga maritima MSB8

Interaction of sulochrin to active site of glucosidase enzyme of Termotoga maritime has been studied by employing docking method using Molecular Operating Environment (MOE), in comparison with those are reports of established inhibitor α-glucosidase such as acarbose, miglitol and voglibose, and salicinol, as reference compounds. The crystal structure T. maritima α-glucanotransferase (PDB code: 1LWJ) can be employed to serve as the template in the virtual screening of S. cerevisiae α-glucosidase. The comparison between the binding pocket residues of Thermotoga maritima α-glucanotransferase and Saccharomyces cerevisiae α-glucosidase show a high sequence identity and similarity. The result showed that sulochrin could be located in the binding pocket and formed some interactions with the binding residues. The ligands showed proper predicted binding energy (-6.74 - -4.13 kcal/mol) and predicted Ki values (0.011 - 0.939 mM). Sulochrin has a possibility to serve as a lead compound in the development of new α-glucosidase inhibitor. Keywords: Docking, sulochrin, α-glucosidase Inhibitor, Thermotoga maritime α-glucotransferase, Saccharomyces cerevisiae α-glucosidase, MOE

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Crystal structure of γ-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 Å resolution

Proteins Structure Function and Bioinformatics ◽

10.1002/prot.10562 ◽

2003 ◽

Vol 54 (1) ◽

pp. 157-161 ◽

Cited By ~ 12

Author(s):

Rebecca Page ◽

Michael S. Nelson ◽

Frank von Delft ◽

Marc-André Elsliger ◽

Jaume M. Canaves ◽

...

Keyword(s):

Crystal Structure ◽

Thermotoga Maritima

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Crystal Structure of RS21-C6, Involved in Nucleoside Triphosphate Pyrophosphohydrolysis

Journal of Molecular Biology ◽

10.1016/j.jmb.2007.01.057 ◽

2007 ◽

Vol 367 (5) ◽

pp. 1405-1412 ◽

Cited By ~ 13

Author(s):

Beili Wu ◽

Yuanfeng Liu ◽

Qiang Zhao ◽

Shuang Liao ◽

Jun Zhang ◽

...

Keyword(s):

Crystal Structure ◽

Nucleoside Triphosphate

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MazG, a Nucleoside Triphosphate Pyrophosphohydrolase, Interacts with Era, an Essential GTPase in Escherichia coli

Journal of Bacteriology ◽

10.1128/jb.184.19.5323-5329.2002 ◽

2002 ◽

Vol 184 (19) ◽

pp. 5323-5329 ◽

Cited By ~ 58

Author(s):

Junjie Zhang ◽

Masayori Inouye

Keyword(s):

Escherichia Coli ◽

Direct Interaction ◽

Kanamycin Resistance ◽

Nucleoside Triphosphate ◽

Cellular Functions ◽

Genomic Libraries ◽

E Coli ◽

Yeast Two Hybrid System ◽

Nucleoside Triphosphate Pyrophosphohydrolase

ABSTRACT Era is an essential GTPase in Escherichia coli, and Era has been implicated in a number of cellular functions. Homologues of Era have been identified in various bacteria and some eukaryotes. Using the era gene as bait in the yeast two-hybrid system to screen E. coli genomic libraries, we discovered that Era interacts with MazG, a protein of unknown function which is highly conserved among bacteria. The direct interaction between Era and MazG was also confirmed in vitro, being stronger in the presence of GDP than in the presence of GTPγS. MazG was characterized as a nucleoside triphosphate pyrophosphohydrolase which can hydrolyze all eight of the canonical ribo- and deoxynucleoside triphosphates to their respective monophosphates and PPi, with a preference for deoxynucleotides. A mazG deletion strain of E. coli was constructed by replacing the mazG gene with a kanamycin resistance gene. Unlike mutT, a gene for another conserved nucleotide triphosphate pyrophosphohydrolase that functions as a mutator gene, the mazG deletion did not result in a mutator phenotype in E. coli.

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