1r1o
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1r1o |SIZE=350|CAPTION= <scene name='initialview01'>1r1o</scene>, resolution 2.8Å | |PDB= 1r1o |SIZE=350|CAPTION= <scene name='initialview01'>1r1o</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> | + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SDC:S-{2-[AMINO(DIHYDROXY)-LAMBDA~4~-SULFANYL]ETHYL}-D-CYSTEINE'>SDC</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </span> |
|GENE= ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1d3v|1D3V]], [[1hq5|1HQ5]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1o OCA], [http://www.ebi.ac.uk/pdbsum/1r1o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r1o RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Christianson, D W.]] | [[Category: Christianson, D W.]] | ||
[[Category: Shin, H.]] | [[Category: Shin, H.]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: SDC]] | ||
[[Category: arginase]] | [[Category: arginase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| Line 33: | Line 34: | ||
[[Category: transition-state analogue]] | [[Category: transition-state analogue]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:22:03 2008'' |
Revision as of 20:22, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | ARG1 (Rattus norvegicus) | ||||||
| Activity: | Arginase, with EC number 3.5.3.1 | ||||||
| Related: | 1D3V, 1HQ5
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Amino Acid Sulfonamides as Transition-State Analogue Inhibitors of Arginase
Overview
Arginase is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of L-arginine to form L-ornithine plus urea. Chiral L-amino acids bearing sulfonamide side chains have been synthesized in which the tetrahedral sulfonamide groups are designed to target bridging coordination interactions with the binuclear manganese cluster in the arginase active site. Syntheses of the amino acid sulfonamides have been accomplished by the amination of sulfonyl halide derivatives of (S)-(tert-butoxy)-[(tert-butoxycarbonyl)amino]oxoalkanoic acids. Amino acid sulfonamides with side chains comparable in length to that of L-arginine exhibit inhibition in the micromolar range, and the X-ray crystal structure of arginase I complexed with one of these inhibitors, S-(2-sulfonamidoethyl)-L-cysteine, has been determined at 2.8 A resolution. In the enzyme-inhibitor complex, the sulfonamide group displaces the metal-bridging hydroxide ion of the native enzyme and bridges the binuclear manganese cluster with an ionized NH(-) group. The binding mode of the sulfonamide inhibitor may mimic the binding of the tetrahedral intermediate and its flanking transition states in catalysis. It is notable that the ionized sulfonamide group is an excellent bridging ligand in this enzyme-inhibitor complex; accordingly, the sulfonamide functionality can be considered in the design of inhibitors targeting other binuclear metalloenzymes.
About this Structure
1R1O is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Design of amino acid sulfonamides as transition-state analogue inhibitors of arginase., Cama E, Shin H, Christianson DW, J Am Chem Soc. 2003 Oct 29;125(43):13052-7. PMID:14570477
Page seeded by OCA on Sun Mar 30 23:22:03 2008
