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PDBsum entry 1kxj
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Contents |
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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The crystal structure of glutamine amidotransferase from thermotoga maritima
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Structure:
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Amidotransferase hish. Chain: a, b. Synonym: glutamine amidotransferase. Engineered: yes
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Source:
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Thermotoga maritima. Organism_taxid: 2336. Gene: hish. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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2.80Å
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R-factor:
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0.229
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R-free:
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0.274
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Authors:
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S.Korolev,T.Skarina,E.Evdokimova,S.Beasley,A.Edwards,A.Joachimiak, A.Savchenko,Midwest Center For Structural Genomics (Mcsg)
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Key ref:
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S.Korolev
et al.
(2002).
Crystal structure of glutamine amidotransferase from Thermotoga maritima.
Proteins,
49,
420-422.
PubMed id:
DOI:
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Date:
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31-Jan-02
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Release date:
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20-Mar-02
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PROCHECK
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Headers
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References
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Q9X0C8
(HIS5_THEMA) -
Imidazole glycerol phosphate synthase subunit HisH from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
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Seq:
Struc:
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201 a.a.
203 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class 2:
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E.C.3.5.1.2
- glutaminase.
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Reaction:
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L-glutamine + H2O = L-glutamate + NH4+
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L-glutamine
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+
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H2O
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=
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L-glutamate
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+
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NH4(+)
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Enzyme class 3:
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E.C.4.3.2.10
- imidazole glycerol-phosphate synthase.
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Reaction:
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5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta- D-ribosyl)imidazole-4-carboxamide + L-glutamine = D-erythro-1-(imidazol- 4-yl)glycerol 3-phosphate + 5-amino-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide + L-glutamate + H+
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5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta- D-ribosyl)imidazole-4-carboxamide
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+
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L-glutamine
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=
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D-erythro-1-(imidazol- 4-yl)glycerol 3-phosphate
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+
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5-amino-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide
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+
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L-glutamate
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proteins
49:420-422
(2002)
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PubMed id:
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Crystal structure of glutamine amidotransferase from Thermotoga maritima.
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S.Korolev,
T.Skarina,
E.Evdokimova,
S.Beasley,
A.Edwards,
A.Joachimiak,
A.Savchenko.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 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.
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Figure 2.
Figure 2. Stereo view of structural comparison of TmHisH (blue
ribbon) and TmHisF (orange ribbon) with His7 (yellow ribbon).
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2002,
49,
420-422)
copyright 2002.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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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?
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Protein Sci,
17,
1120-1128.
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S.Mouilleron,
and
B.Golinelli-Pimpaneau
(2007).
Conformational changes in ammonia-channeling glutamine amidotransferases.
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Curr Opin Struct Biol,
17,
653-664.
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M.Gengenbacher,
T.B.Fitzpatrick,
T.Raschle,
K.Flicker,
I.Sinning,
S.Müller,
P.Macheroux,
I.Tews,
and
B.Kappes
(2006).
Vitamin B6 biosynthesis by the malaria parasite Plasmodium falciparum: biochemical and structural insights.
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J Biol Chem,
281,
3633-3641.
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PDB code:
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M.Strohmeier,
T.Raschle,
J.Mazurkiewicz,
K.Rippe,
I.Sinning,
T.B.Fitzpatrick,
and
I.Tews
(2006).
Structure of a bacterial pyridoxal 5'-phosphate synthase complex.
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Proc Natl Acad Sci U S A,
103,
19284-19289.
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PDB codes:
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M.A.Wilson,
C.V.St Amour,
J.L.Collins,
D.Ringe,
and
G.A.Petsko
(2004).
The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: a member of the DJ-1/ThiJ/PfpI superfamily.
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Proc Natl Acad Sci U S A,
101,
1531-1536.
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PDB codes:
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A.Saeed-Kothe,
and
S.G.Powers-Lee
(2003).
Gain of glutaminase function in mutants of the ammonia-specific frog carbamoyl phosphate synthetase.
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J Biol Chem,
278,
26722-26726.
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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
code is
shown on the right.
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