added two sources on the structure of flavodoxin fold and what is a flavodoxin. Created the structure section of the wiki page, and flavodoxin section
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The '''flavodoxin fold''' is a common [[α/β protein fold]], second only to the [[TIM barrel]] fold. It has three layers, with two [[Alpha helix|α-helical]] layers sandwiching a 5-stranded parallel [[Beta sheet|β-sheet]]. The order of strands within the sheet is 2-1-3-4-5. |
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The '''flavodoxin fold''' is a common [[α/β protein fold]], second only to the [[TIM barrel]] fold. It has three layers, with two [[Alpha helix|α-helical]] layers sandwiching a 5-stranded parallel [[Beta sheet|β-sheet]]. The order of strands within the sheet is 2-1-3-4-5. |
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== Flavodoxin == |
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== Structure == |
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Flavodoxin is a type of protein that is created when iron is low and replaces proteins that contain iron. It is made up of α helices and β sheets. The β-strands are connected by either a loop or an α helix.[{{Cite journal |last=Stultz |first=Collin M. |last2=White |first2=James V. |last3=Smith |first3=Temple F. |date=1993-03 |title=Structural analysis based on state‐space modeling |url=https://onlinelibrary.wiley.com/doi/10.1002/pro.5560020302 |journal=Protein Science |language=en |volume=2 |issue=3 |pages=305–314 |doi=10.1002/pro.5560020302 |issn=0961-8368 |pmc=2142382 |pmid=8453370}}] Flavodoxins contains a singular flavin mononucleotide.[{{Cite web |title=Flavodoxin - an overview {{!}} ScienceDirect Topics |url=https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/flavodoxin |access-date=2026-04-21 |website=www.sciencedirect.com}}] |
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This motif is present for example in lactate dehydrogenase ({{PDB|1A5Z}}) or phosphoglycerate kinase ({{PDB|1FW8}}).[{{cite journal |vauthors=Kalinowska B, Banach M, Wiśniowski Z, Konieczny L, Roterman I |date=July 2017 |title=Is the hydrophobic core a universal structural element in proteins? |journal=Journal of Molecular Modeling |volume=23 |issue=7 |pages=205 |doi=10.1007/s00894-017-3367-z |pmc=5487895 |pmid=28623601}}] |
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This motif is present for example in lactate dehydrogenase ({{PDB|1A5Z}}) or phosphoglycerate kinase ({{PDB|1FW8}}).[{{cite journal |vauthors=Kalinowska B, Banach M, Wiśniowski Z, Konieczny L, Roterman I |date=July 2017 |title=Is the hydrophobic core a universal structural element in proteins? |journal=Journal of Molecular Modeling |volume=23 |issue=7 |pages=205 |doi=10.1007/s00894-017-3367-z |pmc=5487895 |pmid=28623601}}] |
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