4heq: Difference between revisions
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<StructureSection load='4heq' size='340' side='right'caption='[[4heq]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='4heq' size='340' side='right'caption='[[4heq]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4heq]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4heq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Megalodesulfovibrio_gigas Megalodesulfovibrio gigas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HEQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4heq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4heq OCA], [https://pdbe.org/4heq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4heq RCSB], [https://www.ebi.ac.uk/pdbsum/4heq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4heq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/FLAV_MEGG1 FLAV_MEGG1] Electron-transfer proteins that function in various electron transport systems in microorganisms. Functionally interchangeable with ferredoxin. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Flavodoxin|Flavodoxin]] | *[[Flavodoxin 3D structures|Flavodoxin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Megalodesulfovibrio gigas]] | ||
[[Category: | [[Category: Chen CJ]] | ||
[[Category: | [[Category: Hsieh YC]] | ||
Revision as of 11:13, 3 November 2022
The crystal structure of flavodoxin from Desulfovibrio gigasThe crystal structure of flavodoxin from Desulfovibrio gigas
Structural highlights
FunctionFLAV_MEGG1 Electron-transfer proteins that function in various electron transport systems in microorganisms. Functionally interchangeable with ferredoxin. Publication Abstract from PubMedFlavodoxins, which exist widely in microorganisms, have been found in various pathways with multiple physiological functions. The flavodoxin (Fld) containing the cofactor flavin mononucleotide (FMN) from sulfur-reducing bacteria Desulfovibrio gigas (D. gigas) is a short-chain enzyme that comprises 146 residues with a molecular mass of 15 kDa and plays important roles in the electron-transfer chain. To investigate its structure, we purified this Fld directly from anaerobically grown D. gigas cells. The crystal structure of Fld, determined at resolution 1.3 A, is a dimer with two FMN packing in an orientation head to head at a distance of 17 A, which generates a long and connected negatively charged region. Two loops, Thr59-Asp63 and Asp95-Tyr100, are located in the negatively charged region and between two FMN, and are structurally dynamic. An analysis of each monomer shows that the structure of Fld is in a semiquinone state; the positions of FMN and the surrounding residues in the active site deviate. The crystal structure of Fld from D. gigas agrees with a dimeric form in the solution state. The dimerization area, dynamic characteristics and structure variations between monomers enable us to identify a possible binding area for its functional partners. Crystal Structure of Dimeric Flavodoxin from Desulfovibrio gigas Suggests a Potential Binding Region for the Electron-Transferring Partner.,Hsieh YC, Chia TS, Fun HK, Chen CJ Int J Mol Sci. 2013 Jan 15;14(1):1667-83. doi: 10.3390/ijms14011667. PMID:23322018[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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