1HQG
CRYSTAL STRUCTURE OF THE H141C ARGINASE VARIANT COMPLEXED WITH PRODUCTS ORNITHINE AND UREA
1HQG の概要
エントリーDOI | 10.2210/pdb1hqg/pdb |
関連するPDBエントリー | 1rla |
分子名称 | ARGINASE 1, MANGANESE (II) ION, L-ornithine, ... (5 entities in total) |
機能のキーワード | binuclear manganese cluster, product, hydrolase |
由来する生物種 | Rattus norvegicus (Norway rat) |
細胞内の位置 | Cytoplasm: P07824 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 106086.90 |
構造登録者 | Cox, J.D.,Cama, E.,Colleluori, D.M.,Ash, D.E.,Christianson, D.W. (登録日: 2000-12-16, 公開日: 2001-04-04, 最終更新日: 2025-03-26) |
主引用文献 | Cox, J.D.,Cama, E.,Colleluori, D.M.,Pethe, S.,Boucher, J.L.,Mansuy, D.,Ash, D.E.,Christianson, D.W. Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase. Biochemistry, 40:2689-2701, 2001 Cited by PubMed Abstract: Arginase is a binuclear Mn(2+) metalloenzyme that catalyzes the hydrolysis of L-arginine to L-ornithine and urea. X-ray crystal structures of arginase complexed to substrate analogues N(omega)-hydroxy-L-arginine and N(omega)-hydroxy-nor-L-arginine, as well as the products L-ornithine and urea, complete a set of structural "snapshots" along the reaction coordinate of arginase catalysis when interpreted along with the X-ray crystal structure of the arginase-transition-state analogue complex described in Kim et al. [Kim, N. N., Cox, J. D., Baggio, R. F., Emig, F. A., Mistry, S., Harper, S. L., Speicher, D. W., Morris, Jr., S. M., Ash, D. E., Traish, A. M., and Christianson, D. W. (2001) Biochemistry 40, 2678-2688]. Taken together, these structures render important insight on the structural determinants of tight binding inhibitors. Furthermore, we demonstrate for the first time the structural mechanistic link between arginase and NO synthase through their respective complexes with N(omega)-hydroxy-L-arginine. That N(omega)-hydroxy-L-arginine is a catalytic intermediate for NO synthase and an inhibitor of arginase reflects the reciprocal metabolic relationship between these two critical enzymes of L-arginine catabolism. PubMed: 11258880DOI: 10.1021/bi002318+ 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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