2bsa: Difference between revisions
New page: left|200px<br /> <applet load="2bsa" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bsa, resolution 1.92Å" /> '''FERREDOXIN-NADP RED... |
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== | ==Ferredoxin-Nadp Reductase (Mutation: Y 303 S) complexed with NADP== | ||
Ferredoxin-NADP+ reductase (FNR) catalyzes the reduction of NADP+ to NADPH | <StructureSection load='2bsa' size='340' side='right'caption='[[2bsa]], [[Resolution|resolution]] 1.92Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bsa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BSA FirstGlance]. <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]] 1.92Å</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>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=2bsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsa OCA], [https://pdbe.org/2bsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bsa RCSB], [https://www.ebi.ac.uk/pdbsum/2bsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bsa ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FENR_NOSSO FENR_NOSSO] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/2bsa_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bsa ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ferredoxin-NADP+ reductase (FNR) catalyzes the reduction of NADP+ to NADPH in an overall reversible reaction, showing some differences in the mechanisms between cyanobacterial and higher plant FNRs. During hydride transfer it is proposed that the FNR C-terminal Tyr is displaced by the nicotinamide. Thus, this C-terminal Tyr might be involved not only in modulating the flavin redox properties, as already shown, but also in nicotinamide binding and hydride transfer. FNR variants from the cyanobacterium Anabaena in which the C-terminal Tyr has been replaced by Trp, Phe, or Ser have been produced. All FNR variants show enhanced NADP+ and NAD+ binding, especially Tyr303Ser, which correlates with a noticeable improvement of NADH-dependent reactions. Nevertheless, the Tyr303Ser variant shows a decrease in the steady-state kcat value with NADPH. Fast kinetic analysis of the hydride transfer shows that the low efficiency observed for this mutant FNR under steady-state conditions is not due to a lack of catalytic ability but rather to the strong enzyme-coenzyme interaction. Three-dimensional structures for Tyr303Ser and Tyr303Trp variants and its complexes with NADP+ show significant differences between plant and cyanobacterial FNRs. Our results suggest that modulation of coenzyme affinity is highly influenced by the strength of the C-terminus-FAD interaction and that subtle changes between plant and cyanobacterial structures are able to modify the energy of that interaction. Additionally, it is shown that the C-terminal Tyr of FNR lowers the affinity for NADP+/H to levels compatible with steady-state turnover during the catalytic cycle, but it is not involved in the hydride transfer itself. | |||
C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H.,Tejero J, Perez-Dorado I, Maya C, Martinez-Julvez M, Sanz-Aparicio J, Gomez-Moreno C, Hermoso JA, Medina M Biochemistry. 2005 Oct 18;44(41):13477-90. PMID:16216071<ref>PMID:16216071</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Anabaena sp | <div class="pdbe-citations 2bsa" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Gomez-Moreno | <references/> | ||
[[Category: Hermoso | __TOC__ | ||
[[Category: Julvez | </StructureSection> | ||
[[Category: Maya | [[Category: Anabaena sp]] | ||
[[Category: Medina | [[Category: Large Structures]] | ||
[[Category: Perez-Dorado | [[Category: Gomez-Moreno C]] | ||
[[Category: Tejero | [[Category: Hermoso JA]] | ||
[[Category: Julvez MM]] | |||
[[Category: Maya CM]] | |||
[[Category: Medina M]] | |||
[[Category: Perez-Dorado I]] | |||
[[Category: Tejero J]] | |||
Latest revision as of 16:54, 13 December 2023
Ferredoxin-Nadp Reductase (Mutation: Y 303 S) complexed with NADPFerredoxin-Nadp Reductase (Mutation: Y 303 S) complexed with NADP
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFerredoxin-NADP+ reductase (FNR) catalyzes the reduction of NADP+ to NADPH in an overall reversible reaction, showing some differences in the mechanisms between cyanobacterial and higher plant FNRs. During hydride transfer it is proposed that the FNR C-terminal Tyr is displaced by the nicotinamide. Thus, this C-terminal Tyr might be involved not only in modulating the flavin redox properties, as already shown, but also in nicotinamide binding and hydride transfer. FNR variants from the cyanobacterium Anabaena in which the C-terminal Tyr has been replaced by Trp, Phe, or Ser have been produced. All FNR variants show enhanced NADP+ and NAD+ binding, especially Tyr303Ser, which correlates with a noticeable improvement of NADH-dependent reactions. Nevertheless, the Tyr303Ser variant shows a decrease in the steady-state kcat value with NADPH. Fast kinetic analysis of the hydride transfer shows that the low efficiency observed for this mutant FNR under steady-state conditions is not due to a lack of catalytic ability but rather to the strong enzyme-coenzyme interaction. Three-dimensional structures for Tyr303Ser and Tyr303Trp variants and its complexes with NADP+ show significant differences between plant and cyanobacterial FNRs. Our results suggest that modulation of coenzyme affinity is highly influenced by the strength of the C-terminus-FAD interaction and that subtle changes between plant and cyanobacterial structures are able to modify the energy of that interaction. Additionally, it is shown that the C-terminal Tyr of FNR lowers the affinity for NADP+/H to levels compatible with steady-state turnover during the catalytic cycle, but it is not involved in the hydride transfer itself. C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H.,Tejero J, Perez-Dorado I, Maya C, Martinez-Julvez M, Sanz-Aparicio J, Gomez-Moreno C, Hermoso JA, Medina M Biochemistry. 2005 Oct 18;44(41):13477-90. PMID:16216071[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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