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1qg0

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Revision as of 09:56, 15 September 2021

WILD-TYPE PEA FNR

Structural highlights

1qg0 is a 2 chain structure with sequence from Garden pea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FENR1_PEA] May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.

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

The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyzes the production of NADPH during photosynthesis. Whereas the structures of FNRs from spinach leaf and a cyanobacterium as well as many of their homologs have been solved, none of these studies has yielded a productive geometry of the flavin-nicotinamide interaction. Here, we show that this failure occurs because nicotinamide binding to wild type FNR involves the energetically unfavorable displacement of the C-terminal Tyr side chain. We used mutants of this residue (Tyr 308) of pea FNR to obtain the structures of productive NADP+ and NADPH complexes. These structures reveal a unique NADP+ binding mode in which the nicotinamide ring is not parallel to the flavin isoalloxazine ring, but lies against it at an angle of approximately 30 degrees, with the C4 atom 3 A from the flavin N5 atom.

A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies.,Deng Z, Aliverti A, Zanetti G, Arakaki AK, Ottado J, Orellano EG, Calcaterra NB, Ceccarelli EA, Carrillo N, Karplus PA Nat Struct Biol. 1999 Sep;6(9):847-53. PMID:10467097^[1]

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

References

↑ Deng Z, Aliverti A, Zanetti G, Arakaki AK, Ottado J, Orellano EG, Calcaterra NB, Ceccarelli EA, Carrillo N, Karplus PA. A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies. Nat Struct Biol. 1999 Sep;6(9):847-53. PMID:10467097 doi:10.1038/12307

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/1qg0"

@@ Line 3: / Line 3: @@
 <StructureSection load='1qg0' size='340' side='right'caption='[[1qg0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qg0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Garden_pea Garden pea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QG0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QG0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qg0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Garden_pea Garden pea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QG0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] </span></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=1qg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qg0 OCA], [http://pdbe.org/1qg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qg0 RCSB], [http://www.ebi.ac.uk/pdbsum/1qg0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qg0 ProSAT]</span></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=1qg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qg0 OCA], [https://pdbe.org/1qg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qg0 RCSB], [https://www.ebi.ac.uk/pdbsum/1qg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qg0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FENR1_PEA FENR1_PEA]] May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.
+[[https://www.uniprot.org/uniprot/FENR1_PEA FENR1_PEA]] May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1qg0

From Proteopedia

Revision as of 09:56, 15 September 2021

WILD-TYPE PEA FNR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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