3ui5 | pdb_00003ui5

Crystal structure of human Parvulin 14

spinqualitylabelsall models 3ui5, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ui5 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: D1D, NA, SO4 Related: 3ui4, 3ui6 Gene: PIN4, Q9Y237 (Homo sapiens) Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Parvulins compose a family of small peptidyl-prolyl isomerases (PPIases) involved in protein folding and protein quality control. A number of amino acids in the catalytic cavity are highly conserved, but their precise role within the catalytic mechanism is unknown. The 0.8 A crystal structure of the prolyl isomerase domain of parvulin Par14 shows the electron density of hydrogen atoms between the D74, H42, H123, and T118 side chains. This threonine residue has previously not been associated with catalysis, but a corresponding T152A mutant of Pin1 shows a dramatic reduction of catalytic activity without compromising protein stability. The observed catalytic tetrad is strikingly conserved in Pin1- and parvulin-type proteins and hence constitutes a common feature of small peptidyl prolyl isomerases. Crystallographic Proof for an Extended Hydrogen-Bonding Network in Small Prolyl Isomerases.,Mueller JW, Link NM, Matena A, Hoppstock L, Ruppel A, Bayer P, Blankenfeldt W J Am Chem Soc. 2011 Nov 21. PMID:22081960 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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