2zav | pdb_00002zav
Arginase I (homo sapiens): native and unliganded structure at 1.70 A resolution
Structural highlights
DiseaseARGI1_HUMAN Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:207800; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.[1] [2] FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the human arginase I-thiosemicarbazide complex reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster. The C=S moiety of thiosemicarbazide bridges Mn(2+)A and Mn(2+)B with coordination distances of 2.6 A and 2.4 A, respectively. Otherwise, the binding of thiosemicarbazide to human arginase I does not cause any significant structural changes in the active site. The crystal structure of the unliganded enzyme reveals a hydrogen bonded water molecule that could support proton transfer between a mu-water molecule and H141 to regenerate the nucleophilic mu-hydroxide ion in the final step of catalysis. Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster.,Di Costanzo L, Pique ME, Christianson DW J Am Chem Soc. 2007 May 23;129(20):6388-9. doi: 10.1021/ja071567j. Epub 2007 May , 1. PMID:17469833[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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