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Literature summary for 1.4.1.13 extracted from

  • Swuec, P.; Chaves-Sanjuan, A.; Camilloni, C.; Vanoni, M.A.; Bolognesi, M.
    Cryo-EM structures of Azospirillum brasilense glutamate synthase in its oligomeric assemblies (2019), J. Mol. Biol., 431, 4523-4526 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
cryo-electron microscopy structures of GltS in oligomeric states alpha4beta3, alpha4beta4, alpha6beta4 and alpha6beta6, in the 3.5- to 4.1 A resolution range Azospirillum brasilense

Organism

Organism UniProt Comment Textmining
Azospirillum brasilense Q05755 and Q05756 Q05755 i.e. large chain GltB, Q05756 i.e. small chain GltD
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Synonyms

Synonyms Comment Organism
GltS
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Azospirillum brasilense

Cofactor

Cofactor Comment Organism Structure
FAD the isoalloxazine ring is almost solvent inaccessible, neighboring residues are Ile98, Pro100, Leu186, Ile191, Lys195, Leu266, Asp300, Thr301, Asp304, Leu450 and Val451, together with backbone atoms of the surrounding regions Azospirillum brasilense
[4Fe-4S]-center the [4Fe-4S]+1,+2 cluster A displays three Cys and one Glu ligands for the Fe atoms. Residues Cys105 and Cys60 are linked to Fe1 and Fe2, respectively and the Fe3 atom shows bidentate coordination to Glu125 carboxylate, Fe4 is coordinated to Cys99, whose Calpha atom falls 5 A from FAD dimethyl-benzene ring C8 methyl. All Cys ligands to the [4Fe-4S]+1,+2 cluster B (Cys48, Cys51, Cys56, Cys109) are comprised in small subunit GltD loops at the interface with GltB Azospirillum brasilense