... attack on the anomeric carbon of fructose. The leaving group iscarboxylate of Asp54.Dimerization The asymmetric units ofthe crystals of both the apoand complexed formofthe enzyme consist of dimerswith ... maps. The crystal structure ofthe complex of b-fructofura-nosidase with fructose was solved by molecularreplacement using thecrystal structure ofthe nativeenzyme as the search model. The ... blades in the axisarea are of polar character. The water channel in the apo formofthe enzyme runs along the axis of the b-propeller through the whole domain and is onlyblocked by Cys236 in the...
... counted the interactions, we excluded all residuesinvolved in the binding ofthe metal cofactor.ApeSODs in different forms were superimposed with the least square fit of Ca atoms ofthe residues ... ligand,NE2 of His31, bound to the metal, in the company of a water oxygen, from the apical positions. The manga-nese was only 0.06 A˚out ofthe equatorial plane(Table 3). The angles around the metal ... additional water oxy-gen, which, together with the OD2 of Asp165, the NE2 of His79 and the NE2 of His169, formed anequatorial plane (Fig. 3B). The metal ion and the addi-tional water oxygen were...
... regulatory mechanism of Thr and the struc-tural features responsible for the high thermostability of TtAKb.Results and DiscussionModel quality The crystal structure ofthe Thr-bound formof TtAKb(TtAKb-Thr) ... good quality, with 95.4% ofthe res-idues in the most favored regions and 4.6% in allowedregions ofthe Ramachandran plot. The crystal structure ofthe Thr-free formof TtAKb(TtAKb-free) was ... binding shifts the equilibrium to dimer formation. In the absence of Thr, an outwardshift of b-strands near the Thr-binding site (site 1) and a concomitant loss of the electron density ofthe loop...
... Ser214–Gly219 (the entrance frame), Lys224–Tyr228 (the back ofthe pocket) and the disulfide bridgeCys191–Cys220 (the front ofthe pocket) (Fig. 4A). The backbones of these segments form a deep ... below). The southern boundary of the active site cleft of DESC1 is formed by the 145autolysis loop. The backbone of this loop differs mark-edly from the other serine proteinases, making the act-ive ... revealsthat the most similar regions of these proteinases medi-ate interaction ofthe two b-barrels, formation of the catalytic machinery and structures required for binding of the main chain of the...
... active site formation. Sections (6 A˚thick) ofthe protein surface that illustrate the shape and size of the active site. The sphere represents the zinc ion. (A) The main body of the active ... acetatewhich is the product of a deacetylation reaction. (c) The protein forms stable homohexamers both in the crystal form and in solution. Thus, the functionalstate ofthe enzyme is probably the hexamer. ... determines the shape of the active site entry. (e) The structure ofthe active site isessentially identical with the active sites ofthe MshBand LpxC proteins. The conservation of catalyticallyimportant...
... the Cys73–Cys73 disulfide bond [23]. The substitution of thesehydrogen bond forming residues in hTRXL-N may accountfor the formation of a monomer, instead of a dimer in the case of TRX. Furthermore, ... dissimilar crystal forms anddissimilar intermolecular contacts near the active site in the crystal, the conformation ofthe active site (-Cys-Gly-Pro-Cys-) ofthe hTRXL-N determined in the present ... little directeffect on the activity ofthe enzyme. The function of thisunique C-terminal domain remains unknown.Overall structureCrystals ofthe catalytic domain of hTRXL (hTRXL-N)were obtained...
... part, and (b) the variability ofthe angle of approach ofthe inhibitor relative to the catalyticcleft ofthe enzyme. The latter factor may reflect notso much the geometry ofthe catalytic site ... PW),despite the lack of overall sequence similarity. The role ofthe proline residue appears to be to maintain the specific shape ofthe loop. The aromatic residue,on the other hand, interacts with the ... [20,21]. The other segment ofthe guanidinium group of R91forms a pair of hydrogen bonds with the oxygen atom of the side-chain amide group of N18e. It is interestingto note that the equivalent...
... subunits of both crystal forms (diagonalterms). Please note the symmetry ofcrystalform 1 and asymmetry of crystalform 2 represented by low and high values ofthe rmsd,respectively.Subunita Crystal ... In the center there is a schematic of the mutual relationship ofthe monomers,in selected members ofthe family, as indi-cated by the twist angle ofthe dimer.TM1415 constitutes one ofthe ... 1. Schematic ofthe transformation of TM1415 into the eukaryotic FBPase. The transformation requires 25° rotation of the dimers around the tetramer axis and 30°rotation ofthe monomers in...
... but,like the d and d¢ subunits ofthe clamp-loader, neither vnor w contain any ofthe functional elements required fornucleotide binding. The topology ofthe w subunitresembles that ofthe bacterial ... of w,fromthelistofsequencesgiveninTable 3, is shown. The alignment is colored according to the degree of sequence conservation. These 26 residues are disordered in the crystal structure ofthe ... protein via the distal surface of v. The base ofthe clamp-loader complex hasan open C-shaped structure, and the shape ofthe v:w com-plex is suggestive of a loose docking within the crevice formedby...
... molecule to form an isopeptide bond with the Gly93 of another. The crystal structures of diubiquitin and tetraubiquitinshowed some alternatives ofthe quaternary c onformations of ubiquitin ... chains, theirconformations were adjusted with reference t o the NMRstructure of SUMO-1 and thecrystal structure of yeastACDBFig. 2. Photographs and electron density maps ofthe SUMO-2 crystals. ... residues 45–58 in the former model and 40 , 49 and 55–58 in the latter model of SUMO-2 and the equivalents of ubiquitin. Although the sequences have only 18% identity, the protein folds of SUMO-2 and...
... live in a snake.14. My brother managed to kill the snake just at the time when I were almost exhausted. Supply the correct formofthe verbs1. Cats could fly if they (have) wings.2. If Peter ... (not,want) to live in a snake.14. My brother managed to kill the snake just at the time when I (be) almost exhausted. Ifhe (be) a little late, I (kill) by the snake.15. Had I know you were ill, ... snake.14. My brother managed to kill the snake just at the time when I (be) had been almost exhausted. If he (be) had been a little late, I (kill) would have been killed by the snake.15. Had...
... after the transition ofthe enzyme to amore active form, respectively, t is the time and s is the lag-time. The rate constant, k, for the activation ofthe enzyme isobtained as 1 ⁄ s.CrystallizationCrystals ... lip prevented binding ofthe C-terminalresidues over the active site, or the absence of the C-terminal residues caused the movement ofthe lip(Fig. 1B). In addition, the Cachain between aminoacid ... between the dCTP(dUTP)-bindingconformer and the dTTP-binding conformer of dCTPdeaminase. We were not able to identify structuralchanges in the main chain ofthe subunit, or in the interaction of...