1w7c: Difference between revisions

New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1w7c.gif|left|200px]]<br /><applet load="1w7c" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1w7c, resolution 1.23&Aring;" />
caption="1w7c, resolution 1.23&Aring;" />
'''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, 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 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W7C OCA].  
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.E.]]
[[Category: Cohen, A E.]]
[[Category: Duff, A.P.]]
[[Category: Duff, A P.]]
[[Category: Ellis, P.J.]]
[[Category: Ellis, P J.]]
[[Category: Guss, J.M.]]
[[Category: Guss, J M.]]
[[Category: CA]]
[[Category: CA]]
[[Category: CL]]
[[Category: CL]]
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[[Category: tpq]]
[[Category: tpq]]


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