scholarly journals The crystal structure of Aq_328 from the hyperthermophilic bacteria Aquifex aeolicus shows an ancestral histone fold

2005 ◽  
Vol 62 (1) ◽  
pp. 8-16 ◽  
Author(s):  
Yang Qiu ◽  
Valentina Tereshko ◽  
Youngchang Kim ◽  
Rongguang Zhang ◽  
Frank Collart ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Aquifex Aeolicus ◽  
Histone Fold ◽  
Hyperthermophilic Bacteria

Crystal structure of Aquifex aeolicus gene product Aq1627: a putative phosphoglucosamine mutase reveals a unique C-terminal end-to-end disulfide linkage

2017 ◽  
Vol 13 (7) ◽  
pp. 1370-1376
Author(s):  
Upasana Sridharan ◽  
Seiki Kuramitsu ◽  
Shigeyuki Yokoyama ◽  
Thirumananseri Kumarevel ◽  
Karthe Ponnuraj
Keyword(s):  
Crystal Structure ◽  
Gene Product ◽  
Aquifex Aeolicus ◽  
Disulfide Linkage ◽  
Hyperthermophilic Bacterium ◽  
End To End

The crystal structure of Aq1627 protein from Aquifex aeolicus, a hyperthermophilic bacterium has been solved, which reveals a unique end-to-end disulfide linkage.

Crystal structure of ribosomal protein L1 from the bacterium Aquifex aeolicus

2011 ◽  
Vol 56 (4) ◽  
pp. 603-607 ◽  
Author(s):  
E. Yu. Nikonova ◽  
S. V. Tishchenko ◽  
A. G. Gabdulkhakov ◽  
A. A. Shklyaeva ◽  
M. B. Garber ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ribosomal Protein ◽  
Aquifex Aeolicus ◽  
Ribosomal Protein L1

scholarly journals Leucyl-tRNA Synthetase Consisting of Two Subunits from Hyperthermophilic Bacteria Aquifex aeolicus

2002 ◽  
Vol 277 (44) ◽  
pp. 41590-41596 ◽  
Author(s):  
Min-Gang Xu ◽  
Jian-Feng Chen ◽  
Franck Martin ◽  
Ming-Wei Zhao ◽  
Gilbert Eriani ◽  
...  
Keyword(s):  
Trna Synthetase ◽  
Aquifex Aeolicus ◽  
Hyperthermophilic Bacteria

scholarly journals Crystal Structure of tRNA Adenosine Deaminase (TadA) fromAquifex aeolicus

2005 ◽  
Vol 280 (16) ◽  
pp. 16002-16008 ◽  
Author(s):  
Mitsuo Kuratani ◽  
Ryohei Ishii ◽  
Yoshitaka Bessho ◽  
Ryuya Fukunaga ◽  
Toru Sengoku ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Adenosine Deaminase ◽  
Cytosine Deaminase ◽  
Amino Acid Residues ◽  
Aquifex Aeolicus ◽  
Stem Loop ◽  
Dimeric Structure ◽  
Docking Model ◽  
Tetrameric Structure ◽  
Yeast Cytosine Deaminase

The bacterial tRNA adenosine deaminase (TadA) generates inosine by deaminating the adenosine residue at the wobble position of tRNAArg-2. This modification is essential for the decoding system. In this study, we determined the crystal structure ofAquifex aeolicusTadA at a 1.8-Å resolution. This is the first structure of a deaminase acting on tRNA.A. aeolicusTadA has an α/β/α three-layered fold and forms a homodimer. TheA. aeolicusTadA dimeric structure is completely different from the tetrameric structure of yeast CDD1, which deaminates mRNA and cytidine, but is similar to the dimeric structure of yeast cytosine deaminase. However, in theA. aeolicusTadA structure, the shapes of the C-terminal helix and the regions between the β4 and β5 strands are quite distinct from those of yeast cytosine deaminase and a large cavity is produced. This cavity contains many conserved amino acid residues that are likely to be involved in either catalysis or tRNA binding. We made a docking model of TadA with the tRNA anticodon stem loop.

scholarly journals Crystal Structure of the “PhoU-Like” Phosphate Uptake Regulator from Aquifex aeolicus

2005 ◽  
Vol 187 (12) ◽  
pp. 4238-4244 ◽  
Author(s):  
Vaheh Oganesyan ◽  
Natalia Oganesyan ◽  
Paul D. Adams ◽  
Jaru Jancarik ◽  
Hisao A. Yokota ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Sequence Similarity ◽  
Coiled Coil ◽  
Regulatory Function ◽  
Aquifex Aeolicus ◽  
Ribosome Recycling Factor ◽  
Hsp70 Family ◽  
The One ◽  
Almost All

ABSTRACT The phoU gene of Aquifex aeolicus encodes a protein called PHOU_AQUAE with sequence similarity to the PhoU protein of Escherichia coli. Despite the fact that there is a large number of family members (more than 300) attributed to almost all known bacteria and despite PHOU_AQUAE's association with the regulation of genes for phosphate metabolism, the nature of its regulatory function is not well understood. Nearly one-half of these PhoU-like proteins, including both PHOU_AQUAE and the one from E. coli, form a subfamily with an apparent dimer structure of two PhoU domains on the basis of their amino acid sequence. The crystal structure of PHOU_AQUAE (a 221-amino-acid protein) reveals two similar coiled-coil PhoU domains, each forming a three-helix bundle. The structures of PHOU_AQUAE proteins from both a soluble fraction and refolded inclusion bodies (at resolutions of 2.8 and 3.2Å, respectively) showed no significant differences. The folds of the PhoU domain and Bag domains (for a class of cofactors of the eukaryotic chaperone Hsp70 family) are similar. Accordingly, we propose that gene regulation by PhoU may occur by association of PHOU_AQUAE with the ATPase domain of the histidine kinase PhoR, promoting release of its substrate PhoB. Other proteins that share the PhoU domain fold include the coiled-coil domains of the STAT protein, the ribosome-recycling factor, and structural proteins like spectrin.

Free and ATP-bound structures of Ap4A hydrolase fromAquifex aeolicusV5

2010 ◽  
Vol 66 (2) ◽  
pp. 116-124 ◽  
Author(s):  
Jeyaraman Jeyakanthan ◽  
Shankar Prasad Kanaujia ◽  
Yuya Nishida ◽  
Noriko Nakagawa ◽  
Surendran Praveen ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Conformational Changes ◽  
Active Site ◽  
Three Dimensional ◽  
Protein Molecule ◽  
Water Molecules ◽  
Aquifex Aeolicus ◽  
Functional Roles ◽  
Product Molecule ◽  
Dimensional Crystal

Asymmetric diadenosine tetraphosphate (Ap4A) hydrolases degrade the metabolite Ap4A back into ATP and AMP. The three-dimensional crystal structure of Ap4A hydrolase (16 kDa) fromAquifex aeolicushas been determined in free and ATP-bound forms at 1.8 and 1.95 Å resolution, respectively. The overall three-dimensional crystal structure of the enzyme shows an αβα-sandwich architecture with a characteristic loop adjacent to the catalytic site of the protein molecule. The ATP molecule is bound in the primary active site and the adenine moiety of the nucleotide binds in a ring-stacking arrangement equivalent to that observed in the X-ray structure of Ap4A hydrolase fromCaenorhabditis elegans. Binding of ATP in the active site induces local conformational changes which may have important implications in the mechanism of substrate recognition in this class of enzymes. Furthermore, two invariant water molecules have been identified and their possible structural and/or functional roles are discussed. In addition, modelling of the substrate molecule at the primary active site of the enzyme suggests a possible path for entry and/or exit of the substrate and/or product molecule.

scholarly journals Crystal structure of conserved hypothetical protein Aq1575 from Aquifex aeolicus

2002 ◽  
Vol 99 (12) ◽  
pp. 7980-7985 ◽  
Author(s):  
D. H. Shin ◽  
H. Yokota ◽  
R. Kim ◽  
S.-H. Kim
Keyword(s):  
Crystal Structure ◽  
Hypothetical Protein ◽  
Aquifex Aeolicus

The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex aeolicus at 1.7Å Resolution

2005 ◽  
Vol 348 (3) ◽  
pp. 535-547 ◽  
Author(s):  
Philip D. Martin ◽  
Cristina Purcarea ◽  
Pengfei Zhang ◽  
Asmita Vaishnav ◽  
Sharon Sadecki ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Aquifex Aeolicus

Crystal Structure of the Bifunctional ATP Sulfurylase – APS kinase from the Chemolithotrophic Thermophile Aquifex aeolicus

2007 ◽  
Vol 365 (3) ◽  
pp. 732-743 ◽  
Author(s):  
Zhihao Yu ◽  
Eric B. Lansdon ◽  
Irwin H. Segel ◽  
Andrew J. Fisher
Keyword(s):  
Crystal Structure ◽  
Aquifex Aeolicus ◽  
Atp Sulfurylase ◽  
Aps Kinase
Sign in / Sign up

Export Citation Format

Share Document