Aspartate Transcarbamylase from the Hyperthermophilic Archaeon Pyrococcus abyssi: Thermostability and 1.8Å Resolution Crystal Structure of the Catalytic Subunit Complexed With the Bisubstrate Analogue N-Phosphonacetyl-l-aspartate

Structural Investigation of Cold Activity and Regulation of Aspartate Carbamoyltransferase from the Extreme Psychrophilic Bacterium Moritella profunda

“…Ion pair networks, proposed to be major thermostabilizing elements in both hyperthermophilic ATCase crystal structures, 15,16 do not seem to be reduced in the cold active enzyme. We did find a potential role for electrostatics in that the higher glutamate content of the catalytic chains results in more (negative) surface charges that are not involved in salt links.…”

“…12,13 Two hyperthermophilic class B ATCases were recently analyzed structurally and functionally. [14][15][16] Here we report the first crystal structure of a (class B) ATCase from a cold-adapted organism, Moritella profunda (MpATC), in combination with its steady-state kinetics and allosteric behavior.…”

Detecting the Coevolution in and among Protein Domains

“…Other functional sites overlapped with, or close to coevolving positions, include ADP binding sites in carbamoyl-phosphate synthase [30]; Mg 2þ /pyruvate and nucleotide binding sites of PEP utilizing enzyme [31]; NAD, GLU binding sites, and active site of glutamate/leucine/phenylalanine/valine dehydrogenase [32]; nucleotide and sodarin binding sites of elongation factor [33]; active site of aspartate/ornithine carbamoyltransferase [34]; active site of malic enzyme [35]; NADH binding site of S-adenosyl-L-homocysteine hydrolase [36]; GDP-mannuronic acid binding site of UDP-glucose/ GDP-mannose dehydrogenase [37]; and mannitol and NADH binding sites of mannitol dehydrogenase [38]. The annotations of the coevolving sites on the PDB structures of all 25 protein families are given in Text S2.…”

Structure of the catalytic trimer ofMethanococcus jannaschiiaspartate transcarbamoylase in an orthorhombic crystal form

“…PDB codes used were M. jannaschii monoclinic form, 2rgw (Vitali et al, 2008); E. coli catalytic trimer, 3csu (Beernink et al, 1999); P. abyssi catalytic trimer + PALA, 1ml4 (Van Boxstael et al, 2003); E. coli catalytic trimer + PALA, 1ekx (Endrizzi et al, 2000); S. acidocaldarius T-form ATCase, 1pg5 (De Vos et al, 2004); E. coli T-form ATCase, 6at1 (Stevens et al, 1990a,b); E. coli R-form ATCase, 1d09 (Jin et al, 1999). Values for crystallographically independent chains are separated by commas.…”

“…This study and comparisons with E. coli ATCase and the hyperthermophilic ATCases from Pyrococcus abyssi (Van Boxstael et al, 2003) and Sulfolobus acidocaldarius (De Vos et al, 2004) provided insight into the strategies for thermostabilization adopted by the M. jannaschii enzyme. We undertook the structural analysis of the orthorhombic form which is presented in this paper in order to further investigate the structure of the enzyme in different crystalline environments and its thermostabilization strategies.…”