2ZAV

Arginase I (homo sapiens): native and unliganded structure at 1.70 A resolution

Summary for 2ZAV

• Entry DOI: 10.2210/pdb2zav/pdb
• Related: 2PHA
• Descriptor: Arginase-1, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: manganese cluster coordination, proton wire, apical water, alternative splicing, arginine metabolism, cytoplasm, disease mutation, hydrolase, metal-binding, phosphorylation, polymorphism, urea cycle
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P05089
• Total number of polymer chains: 2
• Total formula weight: 69779.51

Authors

Di Costanzo, L.,Christianson, D.W. (deposition date: 2007-10-11, release date: 2007-10-30, Last modification date: 2023-11-01)

Primary citation

Di Costanzo, L.,Pique, M.E.,Christianson, D.W.
Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster
J.Am.Chem.Soc., 129:6388-6389, 2007

PubMed Abstract: The crystal structure of the human arginase I-thiosemicarbazide complex reveals an unusual thiocarbonyl μ-sulfide ligand in the binuclear manganese cluster. The C=S moiety of thiosemicarbazide bridges MnA and MnB with coordination distances of 2.6 Å and 2.4 Å, 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 μ-water molecule and H141 to regenerate the nucleophilic μ-hydroxide ion in the final step of catalysis.

PubMed: 17469833
DOI: 10.1021/ja071567j

Experimental method

X-RAY DIFFRACTION (1.7 Å)