scholarly journals Crystal Structure of Butyrate Kinase 2 from Thermotoga maritima, a Member of the ASKHA Superfamily of Phosphotransferases

2012 ◽  
Vol 194 (11) ◽  
pp. 3033-3033
Author(s):  
J. Diao ◽  
M. S. Hasson
Keyword(s):  
Crystal Structure ◽  
Thermotoga Maritima ◽  
Butyrate Kinase

scholarly journals Crystal Structure of Butyrate Kinase 2 from Thermotoga maritima, a Member of the ASKHA Superfamily of Phosphotransferases

2009 ◽  
Vol 191 (8) ◽  
pp. 2521-2529 ◽  
Author(s):  
Jiasheng Diao ◽  
Miriam S. Hasson
Keyword(s):  
Crystal Structure ◽  
Substrate Specificity ◽  
Active Site ◽  
Thermotoga Maritima ◽  
Structural Basis ◽  
Acetate Kinase ◽  
Phosphoryl Transfer ◽  
Atp Binding ◽  
Binding Motif ◽  
Butyrate Kinase

ABSTRACT The enzymatic transfer of phosphoryl groups is central to the control of many cellular processes. One of the phosphoryl transfer mechanisms, that of acetate kinase, is not completely understood. Besides better understanding of the mechanism of acetate kinase, knowledge of the structure of butyrate kinase 2 (Buk2) will aid in the interpretation of active-site structure and provide information on the structural basis of substrate specificity. The gene buk2 from Thermotoga maritima encodes a member of the ASKHA (acetate and sugar kinases/heat shock cognate/actin) superfamily of phosphotransferases. The encoded protein Buk2 catalyzes the phosphorylation of butyrate and isobutyrate. We have determined the 2.5-Å crystal structure of Buk2 complexed with (β,γ-methylene) adenosine 5′-triphosphate. Buk2 folds like an open-shelled clam, with each of the two domains representing one of the two shells. In the open active-site cleft between the N- and C-terminal domains, the active-site residues consist of two histidines, two arginines, and a cluster of hydrophobic residues. The ATP binding region of Buk2 in the C-terminal domain consists of abundant glycines for nucleotide binding, and the ATP binding motif is similar to those of other members of the ASKHA superfamily. The enzyme exists as an octamer, in which four disulfide bonds form between intermolecular cysteines. Sequence alignment and structure superposition identify the simplicity of the monomeric Buk2 structure, a probable substrate binding site, the key residues in catalyzing phosphoryl transfer, and the substrate specificity differences among Buk2, acetate, and propionate kinases. The possible enzyme mechanisms are discussed.

Crystal Structure of Full Length Topoisomerase I from Thermotoga maritima

2006 ◽  
Vol 358 (5) ◽  
pp. 1328-1340 ◽  
Author(s):  
Guido Hansen ◽  
Axel Harrenga ◽  
Bernd Wieland ◽  
Dietmar Schomburg ◽  
Peter Reinemer
Keyword(s):  
Crystal Structure ◽  
Topoisomerase I ◽  
Thermotoga Maritima ◽  
Full Length

scholarly journals THE APPLICABILITY OF THE CRYSTAL STRUCTURE OF TERMOTOGA MARITIMA 4--GLUCANOTRANSFERASE AS THE TEMPLATE FOR SULOCHRIN AS -GLUCOSIDASE INHIBITORS

2010 ◽  
Vol 9 (3) ◽  
pp. 479-486
Author(s):  
Rizna Triana Dewi ◽  
Yulia Anita ◽  
Enade Perdana Istyastono ◽  
Akhmad Darmawan ◽  
Muhamad Hanafi
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Thermotoga Maritima ◽  
Binding Pocket ◽  
Operating Environment ◽  
High Sequence Identity ◽  
Glucosidase Inhibitor ◽  
Glucosidase Inhibitors ◽  
Docking Method ◽  
Binding Residues

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

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

2003 ◽  
Vol 54 (1) ◽  
pp. 157-161 ◽  
Author(s):  
Rebecca Page ◽  
Michael S. Nelson ◽  
Frank von Delft ◽  
Marc-André Elsliger ◽  
Jaume M. Canaves ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Thermotoga Maritima

scholarly journals Crystal structure of a tandem cystathionine-β-synthase (CBS) domain protein (TM0935) from Thermotoga maritima at 1.87 Å resolution

2004 ◽  
Vol 57 (1) ◽  
pp. 213-217 ◽  
Author(s):  
Mitchell D. Miller ◽  
Robert Schwarzenbacher ◽  
Frank von Delft ◽  
Polat Abdubek ◽  
Eileen Ambing ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Thermotoga Maritima ◽  
Cbs Domain ◽  
Domain Protein

scholarly journals Crystal structure of an orphan protein (TM0875) from Thermotoga maritima at 2.00-Å resolution reveals a new fold

2004 ◽  
Vol 56 (3) ◽  
pp. 607-610 ◽  
Author(s):  
Constantina Bakolitsa ◽  
Robert Schwarzenbacher ◽  
Daniel McMullan ◽  
Linda S. Brinen ◽  
Jaume M. Canaves ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Thermotoga Maritima

Structure of nondiscriminating glutamyl-tRNA synthetase fromThermotoga maritima

2010 ◽  
Vol 66 (7) ◽  
pp. 813-820 ◽  
Author(s):  
Takuhiro Ito ◽  
Noriko Kiyasu ◽  
Risa Matsunaga ◽  
Seizo Takahashi ◽  
Shigeyuki Yokoyama
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Thermotoga Maritima ◽  
Trna Synthetase ◽  
Characteristic Structure ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Rossmann Fold

Aminoacyl-tRNA synthetases produce aminoacyl-tRNAs from the substrate tRNA and its cognate amino acid with the aid of ATP. Two types of glutamyl-tRNA synthetase (GluRS) have been discovered: discriminating GluRS (D-GluRS) and nondiscriminating GluRS (ND-GluRS). D-GluRS glutamylates tRNAGluonly, while ND-GluRS glutamylates both tRNAGluand tRNAGln. ND-GluRS produces the intermediate Glu-tRNAGln, which is converted to Gln-tRNAGlnby Glu-tRNAGlnamidotransferase. Two GluRS homologues fromThermotoga maritima, TM1875 and TM1351, have been biochemically characterized and it has been clarified that only TM1875 functions as an ND-GluRS. Furthermore, the crystal structure of theT. maritimaND-GluRS, TM1875, was determined in complex with a Glu-AMP analogue at 2.0 Å resolution. TheT. maritimaND-GluRS contains a characteristic structure in the connective-peptide domain, which is inserted into the catalytic Rossmann-fold domain. The glutamylation ability of tRNAGlnby ND-GluRS was measured in the presence of the bacterial Glu-tRNAGlnamidotransferase GatCAB. Interestingly, the glutamylation efficiency was not affected even in the presence of excess GatCAB. Therefore, GluRS avoids competition with GatCAB and glutamylates tRNAGln.

scholarly journals Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 Å resolution

2004 ◽  
Vol 56 (2) ◽  
pp. 396-400 ◽  
Author(s):  
Glen Spraggon ◽  
Robert Schwarzenbacher ◽  
Andreas Kreusch ◽  
Daniel McMullan ◽  
Linda S. Brinen ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Thermotoga Maritima ◽  
Methionine Aminopeptidase

scholarly journals Crystal structure of a putative glutamine amido transferase (TM1158) from Thermotoga maritima at 1.7 Å resolution

2004 ◽  
Vol 54 (4) ◽  
pp. 801-805 ◽  
Author(s):  
Robert Schwarzenbacher ◽  
Ashley M. Deacon ◽  
Lukasz Jaroszewski ◽  
Linda S. Brinen ◽  
Jaume M. Canaves ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Thermotoga Maritima
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