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| {{STRUCTURE_1w7c| PDB=1w7c | SCENE= }} | | {{STRUCTURE_1w7c| PDB=1w7c | SCENE= }} |
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| '''PPLO AT 1.23 ANGSTROMS'''
| | ===PPLO AT 1.23 ANGSTROMS=== |
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| ==Overview==
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| The structure of Pichia pastoris lysyl oxidase (PPLO) in a new crystal form has been refined at 1.23 Angstrom resolution. PPLO, a copper amine oxidase (CuAO) with a 2,4,5-trihydroxyphenylalanine quinone (TPQ) cofactor, differs from most other members of the CuAO enzyme family in having the ability to oxidize the side chain of lysine residues in a polypeptide. In the asymmetric unit of the crystals, the structure analysis has located residues 43-779 of the polypeptide chain, seven carbohydrate residues, the active-site Cu atom, an imidazole molecule bound at the active site, two buried Ca(2+) ions, five surface Mg(2+) ions, five surface Cl(-) ions and 1045 water molecules. The crystallographic residuals are R = 0.112 and R(free) = 0.146. The TPQ cofactor and several other active-site residues are poorly ordered, in contrast to the surrounding well ordered structure. A covalent cross-link is observed between two lysine residues, Lys778 and Lys66. The cross-link is likely to have been formed by the oxidation of Lys778 followed by a spontaneous reaction with Lys66. The link is modelled as dehydrolysinonorleucine. | | The line below this paragraph, {{ABSTRACT_PUBMED_16929109}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16929109 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16929109}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Topaquinone enzyme]] | | [[Category: Topaquinone enzyme]] |
| [[Category: Tpq]] | | [[Category: Tpq]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:15:30 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:15:32 2008'' |
