1w7c
From Proteopedia
(New page: 200px<br /><applet load="1w7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w7c, resolution 1.23Å" /> '''PPLO AT 1.23 ANGSTRO...) |
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| - | [[Image:1w7c.gif|left|200px]]<br /><applet load="1w7c" size=" | + | [[Image:1w7c.gif|left|200px]]<br /><applet load="1w7c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1w7c, resolution 1.23Å" /> | caption="1w7c, resolution 1.23Å" /> | ||
'''PPLO AT 1.23 ANGSTROMS'''<br /> | '''PPLO AT 1.23 ANGSTROMS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of Pichia pastoris lysyl oxidase (PPLO) in a new crystal | + | 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== | ==About this Structure== | ||
| - | 1W7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_pastoris Pichia pastoris] with NAG, CU, CA, MG, CL, TPQ and IMD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-lysine_6-oxidase Protein-lysine 6-oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.13 1.4.3.13] Full crystallographic information is available from [http:// | + | 1W7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_pastoris Pichia pastoris] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=TPQ:'>TPQ</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-lysine_6-oxidase Protein-lysine 6-oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.13 1.4.3.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein-lysine 6-oxidase]] | [[Category: Protein-lysine 6-oxidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cohen, A | + | [[Category: Cohen, A E.]] |
| - | [[Category: Duff, A | + | [[Category: Duff, A P.]] |
| - | [[Category: Ellis, P | + | [[Category: Ellis, P J.]] |
| - | [[Category: Guss, J | + | [[Category: Guss, J M.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: tpq]] | [[Category: tpq]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:18 2008'' |
Revision as of 13:41, 21 February 2008
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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 with , , , , , and as ligands. Active as Protein-lysine 6-oxidase, with EC number 1.4.3.13 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 Thu Feb 21 15:41:18 2008
Categories: Pichia pastoris | Protein-lysine 6-oxidase | Single protein | Cohen, A E. | Duff, A P. | Ellis, P J. | Guss, J M. | CA | CL | CU | IMD | MG | NAG | TPQ | Amne oxidase | Copper | Oxidase | Oxidoreductase | Quinoprotein | Topaquinone enzyme | Tpq
