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. 2002 Nov 15;49(3):420-2.
doi: 10.1002/prot.10161.

Crystal structure of glutamine amidotransferase from Thermotoga maritima

S Korolev  1 , T Skarina, E Evdokimova, S Beasley, A Edwards, A Joachimiak, A Savchenko
Affiliations

Crystal structure of glutamine amidotransferase from Thermotoga maritima

S Korolev et al. Proteins. .
No abstract available

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Figures

Fig. 1
Fig. 1
Close-up stereo view of active sites residues of TmHisH and TmHisF superimposed with His7. Residues are shown in stick representation with nitrogens, oxygens, and sulfurs shown in blue, red, and yellow, respectively; carbons of His7 residues are shown in gray, carbons of TmHisH are shown in cyan, and carbons of TmHisF are shown in green. TmHisH C84 and His7 C83 with covalent adduct and phosphate (phosphor is shown in orange) are shown in thicker sticks. Labels are shown only for TmHisH and TmHisF residues. 3D structural alignment and all figures were performed with the program ICM.
Fig. 2
Fig. 2
Stereo view of structural comparison of TmHisH (blue ribbon) and TmHisF (orange ribbon) with His7 (yellow ribbon).
See this image and copyright information in PMC

References

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    1. Kuenzler M, Balmelli T, Egli CM, Paravicini G, Braus GH. Cloning, primary structure, and regulation of the His7 gene encoding a bifunctional glutamine amidotransferase: cyclase from Saccharomyces cerevisiae. J Bacteriol. 1993;175:5548–5558. - PMC - PubMed
    1. Klem TJ, Davisson VJ. Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis. Biochemistry. 1993;32:5177–5186. - PubMed
    1. Beismann-Driemeyer S, Sterner R. Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex. J Biol Chem. 2001;276:20387–20396. - PubMed
    1. Lang D, Thoma R, Henn-Sax M, Sterner R, Wilmanns M. Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion. Science. 2000;289:1546–1550. - PubMed

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