PDBsum entry 1k9v

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Transferase PDB id
Protein chain
200 a.a. *
Waters ×65
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Structural evidence for ammonia tunelling across the (beta- alpha)8-barrel of the imidazole glycerol phosphate synthase bienzyme complex
Structure: Amidotransferase hish. Chain: f. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
2.40Å     R-factor:   0.224     R-free:   0.278
Authors: A.Douangamath,M.Walker,S.Beismann-Driemeyer,M.C.Vega- Fernandez,R.Sterner,M.Wilmanns
Key ref:
A.Douangamath et al. (2002). Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex. Structure, 10, 185-193. PubMed id: 11839304 DOI: 10.1016/S0969-2126(02)00702-5
31-Oct-01     Release date:   20-Feb-02    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9X0C8  (HIS5_THEMA) -  Imidazole glycerol phosphate synthase subunit HisH
201 a.a.
200 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     cellular amino acid biosynthetic process   3 terms 
  Biochemical function     transferase activity     3 terms  


DOI no: 10.1016/S0969-2126(02)00702-5 Structure 10:185-193 (2002)
PubMed id: 11839304  
Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex.
A.Douangamath, M.Walker, S.Beismann-Driemeyer, M.C.Vega-Fernandez, R.Sterner, M.Wilmanns.
Since reactive ammonia is not available under physiological conditions, glutamine is used as a source for the incorporation of nitrogen in a number of metabolic pathway intermediates. The heterodimeric ImGP synthase that links histidine and purine biosynthesis belongs to the family of glutamine amidotransferases in which the glutaminase activity is coupled with a subsequent synthase activity specific for each member of the enzyme family. 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. The complex reveals a putative tunnel for the transfer of ammonia over a distance of 25 A. Although ammonia tunneling has been reported for glutamine amidotransferases, the ImGP synthase has evolved a novel mechanism, which extends the known functional properties of the versatile (beta alpha)(8) barrel fold.
  Selected figure(s)  
Figure 1.
Figure 1. Reactions Catalyzed by the Glutaminase Subunit HisH and the Cyclase Subunit HisF, which Constitute the ImGP SynthaseThe products ImGP and AICAR are further used in histidine and de novo purine biosynthesis, respectively.
  The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 185-193) copyright 2002.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20665694 C.Liebold, F.List, H.R.Kalbitzer, R.Sterner, and E.Brunner (2010).
The interaction of ammonia and xenon with the imidazole glycerol phosphate synthase from Thermotoga maritima as detected by NMR spectroscopy.
  Protein Sci, 19, 1774-1782.  
21134639 J.M.Lipchock, and J.P.Loria (2010).
Nanometer propagation of millisecond motions in V-type allostery.
  Structure, 18, 1596-1607.  
20187643 L.Lund, Y.Fan, Q.Shao, Y.Q.Gao, and F.M.Raushel (2010).
Carbamate transport in carbamoyl phosphate synthetase: a theoretical and experimental investigation.
  J Am Chem Soc, 132, 3870-3878.  
19565337 J.Lipchock, and J.P.Loria (2009).
Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima.
  J Biomol NMR, 45, 73-84.  
19670211 R.Koike, A.Kidera, and M.Ota (2009).
Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold.
  Protein Sci, 18, 2060-2066.  
19569682 Y.Fan, L.Lund, Q.Shao, Y.Q.Gao, and F.M.Raushel (2009).
A combined theoretical and experimental study of the ammonia tunnel in carbamoyl phosphate synthetase.
  J Am Chem Soc, 131, 10211-10219.  
18458150 E.J.Hart, and S.G.Powers-Lee (2008).
Mutation analysis of carbamoyl phosphate synthetase: does the structurally conserved glutamine amidotransferase triad act as a functional dyad?
  Protein Sci, 17, 1120-1128.  
19636909 J.M.Lipchock, and J.P.Loria (2008).
1H, 15N and 13C resonance assignment of imidazole glycerol phosphate (IGP) synthase protein HisF from Thermotoga maritima.
  Biomol NMR Assign, 2, 219-221.  
18421771 M.A.Vanoni, and B.Curti (2008).
Structure-function studies of glutamate synthases: a class of self-regulated iron-sulfur flavoenzymes essential for nitrogen assimilation.
  IUBMB Life, 60, 287-300.  
18273849 M.T.Reetz, M.Rentzsch, A.Pletsch, A.Taglieber, F.Hollmann, R.J.Mondière, N.Dickmann, B.Höcker, S.Cerrone, M.C.Haeger, and R.Sterner (2008).
A robust protein host for anchoring chelating ligands and organocatalysts.
  Chembiochem, 9, 552-564.  
17951049 S.Mouilleron, and B.Golinelli-Pimpaneau (2007).
Conformational changes in ammonia-channeling glutamine amidotransferases.
  Curr Opin Struct Biol, 17, 653-664.  
16809541 A.Nakamura, M.Yao, S.Chimnaronk, N.Sakai, and I.Tanaka (2006).
Ammonia channel couples glutaminase with transamidase reactions in GatCAB.
  Science, 312, 1954-1958.
PDB codes: 2df4 2dqn 2f2a 2g5h 2g5i
17144654 F.Zein, Y.Zhang, Y.N.Kang, K.Burns, T.P.Begley, and S.E.Ealick (2006).
Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima.
  Biochemistry, 45, 14609-14620.
PDB code: 2iss
16731983 S.Quevillon-Cheruel, N.Leulliot, M.Graille, K.Blondeau, J.Janin, and H.van Tilbeurgh (2006).
Crystal structure of the yeast His6 enzyme suggests a reaction mechanism.
  Protein Sci, 15, 1516-1521.
PDB code: 2agk
16143853 M.A.Vanoni, L.Dossena, R.H.van den Heuvel, and B.Curti (2005).
Structure-function studies on the complex iron-sulfur flavoprotein glutamate synthase: the key enzyme of ammonia assimilation.
  Photosynth Res, 83, 219-238.  
15849257 R.E.Amaro, R.S.Myers, V.J.Davisson, and Z.A.Luthey-Schulten (2005).
Structural elements in IGP synthase exclude water to optimize ammonia transfer.
  Biophys J, 89, 475-487.  
14585832 J.A.Bauer, E.M.Bennett, T.P.Begley, and S.E.Ealick (2004).
Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5'-phosphate biosynthesis.
  J Biol Chem, 279, 2704-2711.
PDB code: 1r9g
15296735 M.Goto, R.Omi, N.Nakagawa, I.Miyahara, and K.Hirotsu (2004).
Crystal structures of CTP synthetase reveal ATP, UTP, and glutamine binding sites.
  Structure, 12, 1413-1423.
PDB codes: 1vcm 1vcn 1vco
12837772 A.Matte, J.Sivaraman, I.Ekiel, K.Gehring, Z.Jia, and M.Cygler (2003).
Contribution of structural genomics to understanding the biology of Escherichia coli.
  J Bacteriol, 185, 3994-4002.  
12093726 O.Mayans, A.Ivens, L.J.Nissen, K.Kirschner, and M.Wilmanns (2002).
Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry.
  EMBO J, 21, 3245-3254.
PDB codes: 1gxb 1o17
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.