This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1gpj

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Glutamyl-tRNA Reductase from Methanopyrus kandleri

Structural highlights

1gpj is a 1 chain structure with sequence from Methanopyrus kandleri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.95Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HEM1_METKA Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Processes vital to life such as respiration and photosynthesis critically depend on the availability of tetrapyrroles including hemes and chlorophylls. tRNA-dependent catalysis generally is associated with protein biosynthesis. An exception is the reduction of glutamyl-tRNA to glutamate-1-semialdehyde by the enzyme glutamyl-tRNA reductase. This reaction is the indispensable initiating step of tetrapyrrole biosynthesis in plants and most prokaryotes. The crystal structure of glutamyl-tRNA reductase from the archaeon Methanopyrus kandleri in complex with the substrate-like inhibitor glutamycin at 1.9 A resolution reveals an extended yet planar V-shaped dimer. The well defined interactions of the inhibitor with the active site support a thioester-mediated reduction process. Modeling the glutamyl-tRNA onto each monomer reveals an extensive protein-tRNA interface. We furthermore propose a model whereby the large void of glutamyl-tRNA reductase is occupied by glutamate-1-semialdehyde-1,2-mutase, the subsequent enzyme of this pathway, allowing for the efficient synthesis of 5-aminolevulinic acid, the common precursor of all tetrapyrroles.

V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis.,Moser J, Schubert WD, Beier V, Bringemeier I, Jahn D, Heinz DW EMBO J. 2001 Dec 3;20(23):6583-90. PMID:11726494^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Moser J, Lorenz S, Hubschwerlen C, Rompf A, Jahn D. Methanopyrus kandleri glutamyl-tRNA reductase. J Biol Chem. 1999 Oct 22;274(43):30679-85. PMID:10521455
↑ Moser J, Schubert WD, Beier V, Bringemeier I, Jahn D, Heinz DW. V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis. EMBO J. 2001 Dec 3;20(23):6583-90. PMID:11726494 doi:10.1093/emboj/20.23.6583

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gpj"

@@ Line 1: / Line 1: @@
 ==Glutamyl-tRNA Reductase from Methanopyrus kandleri==
-<StructureSection load='1gpj' size='340' side='right' caption='[[1gpj]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<StructureSection load='1gpj' size='340' side='right'caption='[[1gpj]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1gpj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GPJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1gpj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GPJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GMC:(2R,3R,4S,5S)-4-AMINO-2-[6-(DIMETHYLAMINO)-9H-PURIN-9-YL]-5-(HYDROXYMETHYL)TETRAHYDRO-3-FURANOL'>GMC</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpj OCA], [http://pdbe.org/1gpj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gpj RCSB], [http://www.ebi.ac.uk/pdbsum/1gpj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gpj ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GMC:(2R,3R,4S,5S)-4-AMINO-2-[6-(DIMETHYLAMINO)-9H-PURIN-9-YL]-5-(HYDROXYMETHYL)TETRAHYDRO-3-FURANOL'>GMC</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpj OCA], [https://pdbe.org/1gpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gpj RCSB], [https://www.ebi.ac.uk/pdbsum/1gpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gpj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HEM1_METKA HEM1_METKA]] Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.<ref>PMID:10521455</ref>
+[https://www.uniprot.org/uniprot/HEM1_METKA HEM1_METKA] Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.<ref>PMID:10521455</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Methanopyrus kandleri]]
-[[Category: Beier, V]]
+[[Category: Beier V]]
-[[Category: Bringemeier, I]]
+[[Category: Bringemeier I]]
-[[Category: Heinz, D W]]
+[[Category: Heinz DW]]
-[[Category: Jahn, D]]
+[[Category: Jahn D]]
-[[Category: Moser, J]]
+[[Category: Moser J]]
-[[Category: Schubert, W D]]
+[[Category: Schubert W-D]]
-[[Category: Glutamyl trna- reductase]]
-[[Category: Reductase]]
-[[Category: Trna-dependent tetrapyrrole biosynthesis]]

1gpj

From Proteopedia

Current revision

Glutamyl-tRNA Reductase from Methanopyrus kandleri

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox