3b2g: Difference between revisions
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<StructureSection load='3b2g' size='340' side='right'caption='[[3b2g]], [[Resolution|resolution]] 1.76Å' scene=''> | <StructureSection load='3b2g' size='340' side='right'caption='[[3b2g]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3b2g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3b2g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptolyngbya_boryana Leptolyngbya boryana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B2G FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=3b2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b2g OCA], [https://pdbe.org/3b2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b2g RCSB], [https://www.ebi.ac.uk/pdbsum/3b2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b2g 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=3b2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b2g OCA], [https://pdbe.org/3b2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b2g RCSB], [https://www.ebi.ac.uk/pdbsum/3b2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b2g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/FER1_LEPBY FER1_LEPBY] Principal electron carrier in NADP-photoreduction. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Leptolyngbya boryana]] | ||
[[Category: Hase | [[Category: Hase T]] | ||
[[Category: Kurisu | [[Category: Kurisu G]] | ||
Revision as of 11:52, 11 October 2023
Leptolyngbya boryana FerredoxinLeptolyngbya boryana Ferredoxin
Structural highlights
FunctionFER1_LEPBY Principal electron carrier in NADP-photoreduction. Publication Abstract from PubMedFerredoxin (Fd), which plays a pivotal role in photosynthesis as an electron carrier, forms a transient complex with various Fd-dependent enzymes, such as nitrite reductase (NiR), to achieve efficient intermolecular electron transfer. We studied the protein-protein interaction of Fd and NiR by NMR spectroscopy and determined three acidic regions of Fd to be major sites for the interaction with NiR, indicating that the complex is stabilized through electrostatic interaction. During this study, we found Fds from higher plant and cyanobacterium, in spite of their high structural similarities including the above acidic regions, differ remarkably in the interaction with cyanobacterial NiR. In activity assay of NiR, K(m) value for maize Fd (74.6 microM) was 9.6 times larger than that for Leptolyngbya boryana Fd (7.8 microM). The two Fds also showed a similar difference in binding assay to NiR-immobilized resin. Comparative site-specific mutagenesis of two Fds revealed that their discriminative ability for the interaction with NiR is attributed mainly to non-charged residues in the peripheral region of [2Fe-2S] cluster. These non-charged residues are conserved separately between Fds of plant and cyanobacterial origins. Our data highlight that intermolecular force(s) other than electrostatic attraction is(are) also crucial for the molecular interaction between Fd and partner enzyme. A new structural insight into differential interaction of cyanobacterial and plant ferredoxins with nitrite reductase as revealed by NMR and X-ray crystallographic studies.,Sakakibara Y, Kimura H, Iwamura A, Saitoh T, Ikegami T, Kurisu G, Hase T J Biochem. 2012 May;151(5):483-92. Epub 2012 Mar 15. PMID:22427434[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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