1rxx
From Proteopedia
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'''Structure of arginine deiminase''' | '''Structure of arginine deiminase''' | ||
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[[Category: S2F, Structure 2.Function Project.]] | [[Category: S2F, Structure 2.Function Project.]] | ||
[[Category: Sarikaya, E.]] | [[Category: Sarikaya, E.]] | ||
| - | [[Category: | + | [[Category: Arginine degradation pathway]] |
| - | [[Category: | + | [[Category: Catalytic mechanism]] |
| - | [[Category: | + | [[Category: L-arginine deiminase]] |
| - | [[Category: | + | [[Category: S2f]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Structure 2 function project]] |
| - | [[Category: | + | [[Category: X-ray structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:02:28 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:02, 3 May 2008
Structure of arginine deiminase
Overview
l-Arginine deiminase (ADI) catalyzes the irreversible hydrolysis of arginine to citrulline and ammonia. ADI is involved in the first step of the most widespread anaerobic route of arginine degradation. ADI, missing in high eukaryotes, is a potential antimicrobial and antiparasitic drug target. We have determined the crystal structure of ADI from Pseudomonas aeruginosa by the multi-wavelength anomalous diffraction method at 2.45 A resolution. The structure exhibits similarity to other arginine-modifying or substituted arginine-modifying enzymes such as dimethylarginine dimethylaminohydrolase (DDAH), arginine:glycine amidinotransferase, and arginine:inosamine-phosphate amidinotransferase, despite the lack of significant amino acid sequence homology to these enzymes. The similarity spans a core domain comprising five betabetaalphabeta motifs arranged in a circle around a 5-fold pseudosymmetry axis. ADI contains an additional alpha-helical domain of novel topology inserted between the first and the second betabetaalphabeta modules. A catalytic triad, Cys-His-Glu/Asp (arranged in a different manner from that of the thiol proteases), seen in the other arginine-modifying enzymes is also conserved in ADI, as well as many other residues involved in substrate binding. Based on this conservation pattern and the assumption that the substrate binding mode is similar to that of DDAH, an ADI catalytic mechanism is proposed. The main players are Cys-406, which mounts the nucleophilic attack on the carbon atom of the guanidinium group of arginine, and His-278, which serves as a general base.
About this Structure
1RXX is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
Structural insight into arginine degradation by arginine deiminase, an antibacterial and parasite drug target., Galkin A, Kulakova L, Sarikaya E, Lim K, Howard A, Herzberg O, J Biol Chem. 2004 Apr 2;279(14):14001-8. Epub 2003 Dec 30. PMID:14701825 Page seeded by OCA on Sat May 3 08:02:28 2008
Categories: Arginine deiminase | Pseudomonas aeruginosa | Single protein | Galkin, A. | Herzberg, O. | Howard, A. | Kulakova, L. | Lim, K. | S2F, Structure 2.Function Project. | Sarikaya, E. | Arginine degradation pathway | Catalytic mechanism | L-arginine deiminase | S2f | Structural genomic | Structure 2 function project | X-ray structure
