Crystal and molecular structure of bovine 3-hydroxyanthranilic 3, 4-dioxygenase (CROSBI ID 548395)
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Podaci o odgovornosti
Đilović, Ivica ; Matković-Čalogović, Dubravka ; Zanotti, Giuseppe
engleski
Crystal and molecular structure of bovine 3-hydroxyanthranilic 3, 4-dioxygenase
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.
X-ray; molecular structure; 3-hydroxyanthranilic 3; 4-dioxygenase
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Podaci o prilogu
332-x.
2008.
objavljeno
Podaci o matičnoj publikaciji
From Molecules to Medicine: Integrating Crystallography in Drug Discovery
Blundell, Tom
Erice:
Podaci o skupu
International School of Crystallography 40th Course From Molecules to Medicine: Integrating Crystallography in Drug Discovery
poster
29.05.2008-08.06.2008
Erice, Italija