1w7c
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1w7c.gif|left|200px]] | [[Image:1w7c.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1w7c", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1w7c| PDB=1w7c | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''PPLO AT 1.23 ANGSTROMS''' | '''PPLO AT 1.23 ANGSTROMS''' | ||
| Line 30: | Line 27: | ||
[[Category: Ellis, P J.]] | [[Category: Ellis, P J.]] | ||
[[Category: Guss, J M.]] | [[Category: Guss, J M.]] | ||
| - | [[Category: | + | [[Category: Amne oxidase]] |
| - | [[Category: | + | [[Category: Copper]] |
| - | [[Category: | + | [[Category: Oxidase]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Quinoprotein]] |
| - | [[Category: | + | [[Category: Topaquinone enzyme]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 10:15, 3 May 2008
PPLO AT 1.23 ANGSTROMS
Overview
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.
About this Structure
1W7C is a Single protein structure of sequence from Pichia pastoris. Full crystallographic information is available from OCA.
Reference
The 1.23 Angstrom structure of Pichia pastoris lysyl oxidase reveals a lysine-lysine cross-link., Duff AP, Cohen AE, Ellis PJ, Hilmer K, Langley DB, Dooley DM, Freeman HC, Guss JM, Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1073-84. Epub 2006, Aug 19. PMID:16929109 Page seeded by OCA on Sat May 3 13:15:30 2008
