1rxx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1rxx.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1rxx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rxx| PDB=1rxx | SCENE= }}
{{STRUCTURE_1rxx| PDB=1rxx | SCENE= }}
-
'''Structure of arginine deiminase'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14701825}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14701825 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14701825}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Structure 2 function project]]
[[Category: Structure 2 function project]]
[[Category: X-ray structure]]
[[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 Sun Jul 27 23:29:28 2008''

Revision as of 20:29, 27 July 2008

Template:STRUCTURE 1rxx

Structure of arginine deiminase

Template:ABSTRACT PUBMED 14701825

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 Sun Jul 27 23:29:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools