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Gene Review

TM1036  -  imidazole glycerol phosphate synthase...

Thermotoga maritima MSB8

 
 
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Disease relevance of TM1036

  • Its X-ray structure from the hyperthermophile Thermotoga maritima shows that the glutaminase subunit is associated with the N-terminal face of the (beta alpha)(8) barrel cyclase subunit [1].
 

High impact information on TM1036

  • HisH-hisF is a multidomain globular protein complex; hisH is a class I glutamine amidotransferase that hydrolyzes glutamine to form ammonia, and hisF is a (beta/alpha)8 barrel cyclase that completes the ring formation of imidizole glycerol phosphate synthase [2].
  • One hydrogen bond connects the cyclase domain to the substrate analogue in the glutaminase active site [3].
  • N'-((5'-phosphoribosyl)-formimino)-5-aminoimidazol-4-carb oxamid ribonucleotide isomerase crystallised in four different forms, all suitable for X-ray structure solution, and the cyclase moiety of imidazoleglycerol phosphate synthase yielded one crystal form that diffracted to atomic resolution [4].

References

  1. Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex. Douangamath, A., Walker, M., Beismann-Driemeyer, S., Vega-Fernandez, M.C., Sterner, R., Wilmanns, M. Structure (Camb.) (2002) [Pubmed]
  2. Developing an energy landscape for the novel function of a (beta/alpha)8 barrel: ammonia conduction through HisF. Amaro, R., Tajkhorshid, E., Luthey-Schulten, Z. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  3. Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerolphosphate synthase: crystal structures of a ternary complex and the free enzyme. Chaudhuri, B.N., Lange, S.C., Myers, R.S., Davisson, V.J., Smith, J.L. Biochemistry (2003) [Pubmed]
  4. Efficient expression, purification and crystallisation of two hyperthermostable enzymes of histidine biosynthesis. Thoma, R., Obmolova, G., Lang, D.A., Schwander, M., Jenö, P., Sterner, R., Wilmanns, M. FEBS Lett. (1999) [Pubmed]
 
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