1t5f: Difference between revisions
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[[Image:1t5f.gif|left|200px]] | [[Image:1t5f.gif|left|200px]] | ||
'''arginase I-AOH complex''' | {{Structure | ||
|PDB= 1t5f |SIZE=350|CAPTION= <scene name='initialview01'>1t5f</scene>, resolution 2.20Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=DHH:(S)-2-AMINO-7,7-DIHYDROXYHEPTANOIC ACID'>DHH</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] | |||
|GENE= ARG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |||
}} | |||
'''arginase I-AOH complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1T5F is a [ | 1T5F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T5F OCA]. | ||
==Reference== | ==Reference== | ||
Design of amino acid aldehydes as transition-state analogue inhibitors of arginase., Shin H, Cama E, Christianson DW, J Am Chem Soc. 2004 Aug 25;126(33):10278-84. PMID:[http:// | Design of amino acid aldehydes as transition-state analogue inhibitors of arginase., Shin H, Cama E, Christianson DW, J Am Chem Soc. 2004 Aug 25;126(33):10278-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15315440 15315440] | ||
[[Category: Arginase]] | [[Category: Arginase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: arginase]] | [[Category: arginase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:14:02 2008'' | ||
Revision as of 12:14, 20 March 2008
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| 1t5f, resolution 2.20Å | |||||||||||||
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| Ligands: | MN and DHH | ||||||||||||
| Gene: | ARG1 (Rattus norvegicus) | ||||||||||||
| Activity: | Arginase, with EC number 3.5.3.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
arginase I-AOH complex
Overview
Arginase is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to form l-ornithine and urea. Chiral L-amino acids bearing aldehyde side chains have been synthesized in which the electrophilic aldehyde C=O bond is isosteric with the C=N bond of L-arginine. This substitution is intended to facilitate nucleophilic attack by the metal-bridging hydroxide ion upon binding to the arginase active site. Syntheses of the amino acid aldehydes have been accomplished by reduction, oxidation, and Wittig-type reaction with a commercially available derivative of L-glutamic acid. Amino acid aldehydes exhibit inhibition in the micromolar range, and the X-ray crystal structure of arginase I complexed with one of these inhibitors, (S)-2-amino-7-oxoheptanoic acid, has been determined at 2.2 A resolution. In the enzyme-inhibitor complex, the inhibitor aldehyde moiety is hydrated to form the gem-diol: one hydroxyl group bridges the Mn(2+)(2) cluster and donates a hydrogen bond to D128, and the second hydroxyl group donates a hydrogen bond to E277. The binding mode of the neutral gem-diol may mimic the binding of the neutral tetrahedral intermediate and its flanking transition states in arginase catalysis.
About this Structure
1T5F is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Design of amino acid aldehydes as transition-state analogue inhibitors of arginase., Shin H, Cama E, Christianson DW, J Am Chem Soc. 2004 Aug 25;126(33):10278-84. PMID:15315440
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