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4af7

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PEA FNR C266M MUTANT

Structural highlights

4af7 is a 2 chain structure with sequence from Pisum sativum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.85Å
Ligands:
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.

Publication Abstract from PubMed

The role of the highly conserved C266 and L268 of pea ferredoxin-NADP(+) reductase (FNR) in formation of the catalytically competent complex of the enzyme with NADP(H) was investigated. Previous studies suggest that the volume of these side-chains, situated facing the side of the C-terminal Y308 catalytic residue not stacking the flavin isoalloxazine ring, may be directly involved in the fine-tuning of the catalytic efficiency of the enzyme. Wild-type pea FNR as well as single and double mutants of C266 and L268 residues were analysed by fast transient-kinetic techniques and their midpoint reduction potentials were determined. For the C266A, C266M and C266A/L268A mutants a significant reduction in the overall hydride transfer (HT) rates was observed along with the absence of charge-transfer complex formation. The HT rate constants for NADPH oxidation were lower than those for NADP(+) reduction, reaching a 30-fold decrease in the double mutant. In agreement, these variants exhibited more negative midpoint potentials with respect to the wild-type enzyme. The three-dimensional structures of C266M and L268V variants were solved. The C266M mutant shows a displacement of E306 away from the relevant residue S90 to accommodate the bulky methionine introduced. The overall findings indicate that in FNR the volume of the residue at position 266 is essential to attain the catalytic architecture between the nicotinamide and isoalloxazine rings at the active site and, therefore, for an efficient HT process. In addition, flexibility of the 268-270 loop appears to be critical for FNR to achieve catalytically competent complexes with NADP(H).

Structural backgrounds for the formation of a catalytically competent complex with NADP(H) during hydride transfer in ferredoxin-NADP(+) reductases.,Sanchez-Azqueta A, Musumeci MA, Martinez-Julvez M, Ceccarelli EA, Medina M Biochim Biophys Acta. 2012 Apr 20;1817(7):1063-1071. PMID:22542899^[1]

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

References

↑ Sanchez-Azqueta A, Musumeci MA, Martinez-Julvez M, Ceccarelli EA, Medina M. Structural backgrounds for the formation of a catalytically competent complex with NADP(H) during hydride transfer in ferredoxin-NADP(+) reductases. Biochim Biophys Acta. 2012 Apr 20;1817(7):1063-1071. PMID:22542899 doi:10.1016/j.bbabio.2012.04.009

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4af7"

@@ Line 1: / Line 1: @@
 ==PEA FNR C266M MUTANT==
-<StructureSection load='4af7' size='340' side='right' caption='[[4af7]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
+<StructureSection load='4af7' size='340' side='right'caption='[[4af7]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4af7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AF7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AF7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4af7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AF7 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qfy|1qfy]], [[1qga|1qga]], [[2xnc|2xnc]], [[1qfz|1qfz]], [[4af6|4af6]], [[1qg0|1qg0]]</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><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4af7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4af7 OCA], [https://pdbe.org/4af7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4af7 RCSB], [https://www.ebi.ac.uk/pdbsum/4af7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4af7 ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4af7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4af7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4af7 RCSB], [http://www.ebi.ac.uk/pdbsum/4af7 PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
+[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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4af7" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Pisum sativum]]
-[[Category: Ceccarelli, E.]]
+[[Category: Ceccarelli E]]
-[[Category: Martinez-Julvez, M.]]
+[[Category: Martinez-Julvez M]]
-[[Category: Medina, M.]]
+[[Category: Medina M]]
-[[Category: Musumeci, M A.]]
+[[Category: Musumeci MA]]
-[[Category: Sanchez-Azqueta, A.]]
+[[Category: Sanchez-Azqueta A]]
-[[Category: Chloroplast]]
-[[Category: Electron transfer]]
-[[Category: Flavoenzyme]]
-[[Category: Oxidoreductase]]
-[[Category: Photosynthesi]]

4af7

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Current revision

PEA FNR C266M MUTANT

Structural highlights

Function

Publication Abstract from PubMed

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