1hqg

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spinqualitylabelsall models 1hqg, resolution 2.Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE H141C ARGINASE VARIANT COMPLEXED WITH PRODUCTS ORNITHINE AND UREA

Overview

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.

About this Structure

1HQG is a Single protein structure of sequence from Rattus norvegicus with MN, ORN and URE as ligands. Active as Arginase, with EC number 3.5.3.1 Full crystallographic information is available from OCA.

Reference

Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase., Cox JD, Cama E, Colleluori DM, Pethe S, Boucher JL, Mansuy D, Ash DE, Christianson DW, Biochemistry. 2001 Mar 6;40(9):2689-701. PMID:11258880

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