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PDBsum entry 6h0c

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protein ligands metals links
Oxidoreductase PDB id
6h0c

 

 

 

 

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Contents
Protein chain
406 a.a.
Ligands
FLC
Metals
_CL
Waters ×344
PDB id:
6h0c
Name: Oxidoreductase
Title: Flv1 flavodiiron core from synechocystis sp. Pcc6803
Structure: Putative diflavin flavoprotein a 3. Chain: a. Engineered: yes
Source: Synechocystis sp. (Strain pcc 6803 / kazusa). Organism_taxid: 1111708. Strain: pcc 6803 / kazusa. Gene: dfa3, sll1521. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.59Å     R-factor:   0.148     R-free:   0.148
Authors: P.T.Borges,C.V.Romao,L.Saraiva,V.L.Goncalves,M.A.Carrondo,M.Teixeira, C.Frazao
Key ref: P.T.Borges et al. (2019). Analysis of a new flavodiiron core structural arrangement in Flv1-ΔFlR protein from Synechocystis sp. PCC6803. J Struct Biol, 205, 91. PubMed id: 30447285 DOI: 10.1016/j.jsb.2018.11.004
Date:
08-Jul-18     Release date:   30-Jan-19    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P74373  (DFA3_SYNY3) -  Putative diflavin flavoprotein A 3 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Seq:
Struc:
 
Seq:
Struc:
597 a.a.
406 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.1.-.-.-
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/j.jsb.2018.11.004 J Struct Biol 205:91 (2019)
PubMed id: 30447285  
 
 
Analysis of a new flavodiiron core structural arrangement in Flv1-ΔFlR protein from Synechocystis sp. PCC6803.
P.T.Borges, C.V.Romão, L.M.Saraiva, V.L.Gonçalves, M.A.Carrondo, M.Teixeira, C.Frazão.
 
  ABSTRACT  
 
Flavodiiron proteins (FDPs) play key roles in biological response mechanisms against oxygen and/or nitric oxide; in particular they are present in oxygenic phototrophs (including cyanobacteria and gymnosperms). Two conserved domains define the core of this family of proteins: a N-terminal metallo-β-lactamase-like domain followed by a C-terminal flavodoxin-like one, containing the catalytic diiron centre and a FMN cofactor, respectively. Members of the FDP family may present extra modules in the C-terminus, and were classified into several classes according to their distribution and composition. The cyanobacterium Synechocystis sp. PCC6803 contains four Class C FDPs (Flv1-4) that include at the C-terminus an additional NAD(P)H:flavin oxidoreductase (FlR) domain. Two of them (Flv3 and Flv4) have the canonical diiron ligands (Class C, Type 1), while the other two (Flv1 and Flv2) present different residues in that region (Class C, Type 2). Most phototrophs, either Bacterial or Eukaryal, contain at least two FDP genes, each encoding for one of those two types. Crystals of the Flv1 two core domains (Flv1-ΔFlR), without the C-terminal NAD(P)H:flavin oxidoreductase extension, were obtained and the structure was determined. Its pseudo diiron site contains non-canonical basic and neutral residues, and showed anion moieties, instead. The presented structure revealed for the first time the structure of the two-domain core of a Class C-Type 2 FDP.
 

 

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