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1V04

serum paraoxonase by directed evolution

Summary for 1V04
Entry DOI10.2210/pdb1v04/pdb
DescriptorSERUM PARAOXONASE/ARYLESTERASE 1, CALCIUM ION, PHOSPHATE ION, ... (4 entities in total)
Functional Keywordsparaoxonase, hydrolase, directed evolution, antioxidant, israel structural proteomics center, ispc, structural genomics
Biological sourceHOMO SAPIENS
More
Total number of polymer chains1
Total formula weight39779.08
Authors
Harel, M.,Aharoni, A.,Gaidukov, L.,Brumshtein, B.,Khersonsky, O.,Yagur, S.,Meged, R.,Dvir, H.,Ravelli, R.B.G.,McCarthy, A.,Toker, L.,Silman, I.,Sussman, J.L.,Tawfik, D.S. (deposition date: 2004-03-22, release date: 2004-04-23, Last modification date: 2024-10-23)
Primary citationHarel, M.,Aharoni, A.,Gaidukov, L.,Brumshtein, B.,Khersonsky, O.,Meged, R.,Dvir, H.,Ravelli, R.B.G.,Mccarthy, A.,Toker, L.,Silman, I.,Sussman, J.L.,Tawfik, D.S.
Structure and Evolution of the Serum Paraoxonase Family of Detoxifying and Anti-Atherosclerotic Enzymes
Nat.Struct.Mol.Biol., 11:412-, 2004
Cited by
PubMed Abstract: Members of the serum paraoxonase (PON) family have been identified in mammals and other vertebrates, and in invertebrates. PONs exhibit a wide range of physiologically important hydrolytic activities, including drug metabolism and detoxification of nerve agents. PON1 and PON3 reside on high-density lipoprotein (HDL, 'good cholesterol') and are involved in the prevention of atherosclerosis. We describe the first crystal structure of a PON family member, a variant of PON1 obtained by directed evolution, at a resolution of 2.2 A. PON1 is a six-bladed beta-propeller with a unique active site lid that is also involved in HDL binding. The three-dimensional structure and directed evolution studies permit a detailed description of PON1's active site and catalytic mechanism, which are reminiscent of secreted phospholipase A2, and of the routes by which PON family members diverged toward different substrate and reaction selectivities.
PubMed: 15098021
DOI: 10.1038/NSMB767
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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