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Coordination of the ferrous ion in the structure of bovine 3-hydroxyanthranilic 3, 4-dioxygenase


Đilović, Ivica; Matković-Čalogović, Dubravka; Zanotti, Giuseppe
Coordination of the ferrous ion in the structure of bovine 3-hydroxyanthranilic 3, 4-dioxygenase // Seventeenth Slovenian Croatian Crystallographic Meeting / Pevec, Andrej ; Leban, Ivan (ur.).
Ljubljana: Faculty of Chemistry and Chemical Technology University of Ljubljana, 2008. str. 26-26 (predavanje, nije recenziran, sažetak, ostalo)


Naslov
Coordination of the ferrous ion in the structure of bovine 3-hydroxyanthranilic 3, 4-dioxygenase

Autori
Đilović, Ivica ; Matković-Čalogović, Dubravka ; Zanotti, Giuseppe

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, ostalo

Izvornik
Seventeenth Slovenian Croatian Crystallographic Meeting / Pevec, Andrej ; Leban, Ivan - Ljubljana : Faculty of Chemistry and Chemical Technology University of Ljubljana, 2008, 26-26

Skup
Seventeenth Slovenian Croatian Crystallographic Meeting

Mjesto i datum
Ptuj, Slovenija, 19-21.06.2008

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Nije recenziran

Ključne riječi
X-ray; molecular structure; ferrous ion coordination; 3-hydroxyanthranilic 3; 4-dioxygenase

Sažetak
Bovine 3-hydroxyanthranilic 3, 4-dioxygenase (3HAO) is a monomeric cytosolic protein made of 286 residues with a molecular mass of 32542 Da. It catalyzes the synthesis of quinolinic acid from hydroxyanthranilic acid in the kynurenine pathway for the tryptophan catabolism. More specific, it catalyzes the final aromatic ring opening, utilizing non-heme Fe2+ to include both oxygen atoms into product. This pathway is of special interest because quinolinate activates the N-methyl-D-aspartate receptors, which are implicated in several neurological disorders (stroke, epilepsy, Huntington's desease etc.) The structure was determined by the molecular replacement method using a model from the protein data bank (PDB ID: 2QNK1). The overall molecular structure is closely related to those found in various homologues2, 3. The secondary structure is mainly consisted of β strands. Residues His47, His91 and Glu53 are coordinated to the ferrous ion forming part of the active site. The octahedral environment is completed by two water molecules. Oxygen binding site is situated between the Fe2+ ion and Arg 43 residue (plays important role in O− O bond cleavage). Other neighbouring residues form a hydrophobic substrate-binding pocket.

Izvorni jezik
Engleski

Znanstvena područja
Kemija



POVEZANOST RADA


Projekt / tema
119-1193079-1084 - Strukturno istraživanje bioloških makromolekula metodom rentgenske difrakcije (Dubravka Matković-Čalogović, )

Ustanove
Prirodoslovno-matematički fakultet, Zagreb