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PDBsum entry 1o20

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Oxidoreductase PDB id
1o20
Jmol
Contents
Protein chain
414 a.a. *
Waters ×299
* Residue conservation analysis
PDB id:
1o20
Name: Oxidoreductase
Title: Crystal structure of gamma-glutamyl phosphate reductase (tm0 thermotoga maritima at 2.00 a resolution
Structure: Gamma-glutamyl phosphate reductase. Chain: a. Synonym: gpr, glutamate-5-semialdehyde dehydrogenase, gluta semialdehyde dehydrogenase, gsa dehydrogenase. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm0293. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.163     R-free:   0.203
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref:
R.Page et al. (2004). Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 A resolution. Proteins, 54, 157-161. PubMed id: 14705032 DOI: 10.1002/prot.10562
Date:
12-Feb-03     Release date:   01-Apr-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9WYC9  (PROA_THEMA) -  Gamma-glutamyl phosphate reductase
Seq:
Struc:
415 a.a.
414 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.2.1.41  - Glutamate-5-semialdehyde dehydrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Proline Biosynthesis
      Reaction: L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH
L-glutamate 5-semialdehyde
+ phosphate
+ NADP(+)
= L-glutamyl 5-phosphate
+ NADPH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     metabolic process   5 terms 
  Biochemical function     oxidoreductase activity     4 terms  

 

 
    reference    
 
 
DOI no: 10.1002/prot.10562 Proteins 54:157-161 (2004)
PubMed id: 14705032  
 
 
Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 A resolution.
R.Page, M.S.Nelson, F.von Delft, M.A.Elsliger, J.M.Canaves, L.S.Brinen, X.Dai, A.M.Deacon, R.Floyd, A.Godzik, C.Grittini, S.K.Grzechnik, L.Jaroszewski, H.E.Klock, E.Koesema, J.S.Kovarik, A.Kreusch, P.Kuhn, S.A.Lesley, D.McMullan, T.M.McPhillips, M.D.Miller, A.Morse, K.Moy, J.Ouyang, A.Robb, K.Rodrigues, R.Schwarzenbacher, G.Spraggon, R.C.Stevens, H.van den Bedem, J.Velasquez, J.Vincent, X.Wang, B.West, G.Wolf, K.O.Hodgson, J.Wooley, I.A.Wilson.
 
  ABSTRACT  
 

 
  Selected figure(s)  
 
Figure 1.
Figure 1. (A) Ribbon diagram of the TM0293 monomer with its three domains labeled; -helices are in red and -strands are in cyan. The proposed catalytic cysteine, Cys255, is represented in ball-and-stick, with the sulfur in yellow; a prominent difference density around the Cys sulfhydryl group suggests it may be in an oxidized form (density not shown). The NADPH and hinge regions are indicated by arrows, and the N and C termini are labeled. (B) The crystallographic TM0293 tetramer; each monomer is colored separately. (C) Diagram showing the secondary structure elements of TM0293 superimposed on its primary sequence. Helices are labeled H1 to H19. Strands are labeled according to their respective -sheets: A (the oligomerization domain III), B (the cofactor binding domain I), C (the catalytic binding domain II) and D (the hinge). The locations of the hairpin loops, as well as the location of turns and turns, are also depicted in the diagram.
 
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2004, 54, 157-161) copyright 2004.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20091669 I.Pérez-Arellano, F.Carmona-Alvarez, A.I.Martínez, J.Rodríguez-Díaz, and J.Cervera (2010).
Pyrroline-5-carboxylate synthase and proline biosynthesis: from osmotolerance to rare metabolic disease.
  Protein Sci, 19, 372-382.  
18369526 J.J.Tanner (2008).
Structural biology of proline catabolism.
  Amino Acids, 35, 719-730.  
18757760 S.Y.McLoughlin, and S.D.Copley (2008).
A compromise required by gene sharing enables survival: Implications for evolution of new enzyme activities.
  Proc Natl Acad Sci U S A, 105, 13497-13502.  
17064285 S.B.Conners, E.F.Mongodin, M.R.Johnson, C.I.Montero, K.E.Nelson, and R.M.Kelly (2006).
Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
  FEMS Microbiol Rev, 30, 872-905.  
15502869 L.I.Leichert, and U.Jakob (2004).
Protein thiol modifications visualized in vivo.
  PLoS Biol, 2, e333.  
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.