1W1U

Inactive Urocanase-SA cocrystallized with urocanate

1W1U の概要

• エントリーDOI: 10.2210/pdb1w1u/pdb
• 関連するPDBエントリー: 1UWK 1UWL
• 分子名称: UROCANATE HYDRATASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, (2E)-3-(1H-IMIDAZOL-4-YL)ACRYLIC ACID, ... (4 entities in total)
• 機能のキーワード: hydrolase, urocanase, imidazolonepropionate, lyase, histidine metabolism
• 由来する生物種: PSEUDOMONAS PUTIDA
• 細胞内の位置: Cytoplasm: P25080
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 123085.93

構造登録者

Kessler, D.,Retey, J.,Schulz, G.E. (登録日: 2004-06-24, 公開日: 2004-08-19, 最終更新日: 2023-12-13)

主引用文献

Kessler, D.,Retey, J.,Schulz, G.E.
Structure and Action of Urocanase
J.Mol.Biol., 342:183-, 2004

PubMed Abstract: Urocanase (EC 4.2.1.49) from Pseudomonas putida was crystallized after removing one of the seven free thiol groups. The crystal structure was solved by multiwavelength anomalous diffraction (MAD) using a seleno-methionine derivative and then refined at 1.14 A resolution. The enzyme is a symmetric homodimer of 2 x 557 amino acid residues with tightly bound NAD+ cofactors. Each subunit consists of a typical NAD-binding domain inserted into a larger core domain that forms the dimer interface. The core domain has a novel chain fold and accommodates the substrate urocanate in a surface depression. The NAD domain sits like a lid on the core domain depression and points with the nicotinamide group to the substrate. Substrate, nicotinamide and five water molecules are completely sequestered in a cavity. Most likely, one of these water molecules hydrates the substrate during catalysis. This cavity has to open for substrate passage, which probably means lifting the NAD domain. The observed atomic arrangement at the active center gives rise to a detailed proposal for the catalytic mechanism that is consistent with published chemical data. As expected, the variability of the residues involved is low, as derived from a family of 58 proteins annotated as urocanases in the data banks. However, one well-embedded member of this family showed a significant deviation at the active center indicating an incorrect annotation.

PubMed: 15313616
DOI: 10.1016/J.JMB.2004.07.028

実験手法

X-RAY DIFFRACTION (2.23 Å)