Crystal structure of Sulfolobus acidocaldarius aspartate carbamoyltransferase in complex with its allosteric activator CTP

2008 ◽  
Vol 372 (1) ◽  
pp. 40-44 ◽  
Author(s):  
Dirk De Vos ◽  
Ying Xu ◽  
Tony Aerts ◽  
Filip Van Petegem ◽  
Jozef J. Van Beeumen
Keyword(s):  
Crystal Structure ◽  
Sulfolobus Acidocaldarius ◽  
Aspartate Carbamoyltransferase ◽  
Allosteric Activator

Crystal Structure of T State Aspartate Carbamoyltransferase of the Hyperthermophilic Archaeon Sulfolobus acidocaldarius

2004 ◽  
Vol 339 (4) ◽  
pp. 887-900 ◽  
Author(s):  
Dirk De Vos ◽  
Filip Van Petegem ◽  
Han Remaut ◽  
Christianne Legrain ◽  
Nicolas Glansdorff ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sulfolobus Acidocaldarius ◽  
Hyperthermophilic Archaeon ◽  
Aspartate Carbamoyltransferase ◽  
T State

Crystal structure of an Lrs14-like archaeal biofilm regulator fromSulfolobus acidocaldarius

2018 ◽  
Vol 74 (11) ◽  
pp. 1105-1114
Author(s):  
Marian S. Vogt ◽  
Simon L. Völpel ◽  
Sonja-Verena Albers ◽  
Lars-Oliver Essen ◽  
Ankan Banerjee
Keyword(s):  
Crystal Structure ◽  
Biofilm Formation ◽  
Coiled Coil ◽  
Transcriptional Regulators ◽  
Bioinformatic Analysis ◽  
Considerable Degree ◽  
Sulfolobus Acidocaldarius ◽  
Asymmetric Unit ◽  
Winged Helix ◽  
Structural Differences

The small winged helix–turn–helix (wHTH) proteins of the Lrs14 family are major transcriptional regulators and act as archaeal biofilm regulators (AbfRs) in the crenarchaeoteSulfolobus acidocaldarius. Here, the first crystal structure of an AbfR ortholog, AbfR2, the deletion of which is known to impair biofilm formation, is presented. Like most other wHTH orthologs, AbfR2 is dimeric in solution as well as in its 2.45 Å resolution crystal structure. Given the presence of three independent AbfR2 dimers in the asymmetric unit, the crystal structure shows a considerable degree of conformational variation within the dimer, the antiparallel orientations of which are stabilized by coiled-coil interaction between H4 helices. Conserved anchor interactions between helices H0 and H4 of AbfR2 further contribute to dimer stabilization. The combined structural and bioinformatic analysis reveals cluster-specific structural differences between different members of the Lrs14 protein family.

Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 Å resolution 1 1Edited by R. Huber

1999 ◽  
Vol 285 (2) ◽  
pp. 689-702 ◽  
Author(s):  
Stefan Knapp ◽  
Simone Kardinahl ◽  
Niklas Hellgren ◽  
Gudrun Tibbelin ◽  
Günter Schäfer ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Superoxide Dismutase ◽  
Sulfolobus Acidocaldarius ◽  
Hyperthermophilic Archaeon

Leishmania pyruvate kinase: the crystal structure reveals the structural basis of its unique regulatory properties

2000 ◽  
Vol 28 (2) ◽  
pp. 186-190 ◽  
Author(s):  
L. A. Fothergill-Gilmore ◽  
D. J. Rigden ◽  
P. A. M. Michels ◽  
S. E. V. Phillips
Keyword(s):  
Crystal Structure ◽  
Pyruvate Kinase ◽  
Regulatory Role ◽  
Structural Basis ◽  
Protozoan Parasites ◽  
Effector Molecule ◽  
T State ◽  
Regulatory Properties ◽  
Allosteric Activator

Glycolysis occupies a central role in cellular metabolism, and is of particular importance for the catabolic production of ATP in protozoan parasites such as Leishmania and Trypanosoma. In these organisms pyruvate kinase plays a key regulatory role, and is unique in responding to fructose 2,6-bisphosphate as allosteric activator. The determination of the crystal structure of the first eukaryotic pyruvate kinase in the T-state (the inactive or ‘tense’ conformation of allosteric enzymes) is described. A comparison of the effector sites of the Leishmania and yeast enzymes reveals the structural basis for the different effector specificity. Two loops, comprising residues 443–453 and 480–489, adopt very different conformations in the two enzymes, and Lys-453 and His-480 that are a feature of trypanosomatid enzymes provide probable ligands for the 2-phospho group of the effector molecule. These and other differences offer an opportunity for the design of drugs that would exploit regulatory differences between parasite and host.

Escherichia coli aspartate carbamoyltransferase: the probing of crystal structure analysis via site-specific mutagenesis

1991 ◽  
Vol 4 (4) ◽  
pp. 391-408 ◽  
Author(s):  
Raymond C. Stevens ◽  
Yuh Min Chook ◽  
Charles Y. Cho ◽  
William N. Lipscomb ◽  
Evan R. Kantrowitz
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Structure Analysis ◽  
Crystal Structure Analysis ◽  
Site Specific ◽  
Aspartate Carbamoyltransferase

Crystal Structure Determination of Glycerol-Containing Lipids from Electron Diffraction Data. Use of Analog Compounds Based upon Configurational Isomers of Cyclopentane-1, 2, 3-TRIOL

1977 ◽  
Vol 35 ◽  
pp. 24-25
Author(s):  
Douglas L. Dorset ◽  
Anthony J. Hancock
Keyword(s):  
Crystal Structure ◽  
Electron Diffraction ◽  
Diffraction Data ◽  
Structure Determination ◽  
Crystal Surface ◽  
Coherent Scattering ◽  
Crystal Structure Determination ◽  
Electron Diffraction Data ◽  
Polar Group ◽  
Axis Orientation

Lipids containing long polymethylene chains were among the first compounds subjected to electron diffraction structure analysis. It was only recently realized, however, that various distortions of thin lipid microcrystal plates, e.g. bends, polar group and methyl end plane disorders, etc. (1-3), restrict coherent scattering to the methylene subcell alone, particularly if undistorted molecular layers have well-defined end planes. Thus, ab initio crystal structure determination on a given single uncharacterized natural lipid using electron diffraction data can only hope to identify the subcell packing and the chain axis orientation with respect to the crystal surface. In lipids based on glycerol, for example, conformations of long chains and polar groups about the C-C bonds of this moiety still would remain unknown.One possible means of surmounting this difficulty is to investigate structural analogs of the material of interest in conjunction with the natural compound itself. Suitable analogs to the glycerol lipids are compounds based on the three configurational isomers of cyclopentane-1,2,3-triol shown in Fig. 1, in which three rotameric forms of the natural glycerol derivatives are fixed by the ring structure (4-7).

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