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Pregled bibliografske jedinice broj: 396663

Crystal and molecular structure of bovine 3-hydroxyanthranilic 3, 4-dioxygenase


Đilović, Ivica; Matković-Čalogović, Dubravka; Zanotti, Giuseppe
Crystal and molecular structure of bovine 3-hydroxyanthranilic 3, 4-dioxygenase // From Molecules to Medicine: Integrating Crystallography in Drug Discovery / Blundell, Tom (ur.).
Erice, 2008. (poster, nije recenziran, sažetak, ostalo)


Naslov
Crystal and molecular 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
From Molecules to Medicine: Integrating Crystallography in Drug Discovery / Blundell, Tom - Erice, 2008

Skup
International School of Crystallography 40th Course From Molecules to Medicine: Integrating Crystallography in Drug Discovery

Mjesto i datum
Erice, Italija, 29.05.-08.06.2008

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
X-ray; molecular structure; 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. 3HAO is widely distributed in peripheral organs, such as liver and kidney, and is also present in low ammounts in the central nervous system. The structure was determined by the molecular replacement method using model from the protein data bank (PDB ID: 2QNK1). Overall molecular structure is closely related with those found in various homologues2. 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 Fe2+ ion and Arg 43 residue (plays important role in O− O bond cleavage). Other neighbouring residues form hydrophobic substrate-binding pocket. [1] URL: http://www.rcsb.org/pdb/explore/explore.do?structureId=2QNK [2] X. Li et al., Protein Science 15 (2006) 761-773.

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