|
|
| Line 1: |
Line 1: |
| [[Image:2h5u.jpg|left|200px]] | | {{Seed}} |
| | [[Image:2h5u.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2h5u| PDB=2h5u | SCENE= }} | | {{STRUCTURE_2h5u| PDB=2h5u | SCENE= }} |
|
| |
|
| '''Crystal structure of laccase from Cerrena maxima at 1.9A resolution'''
| | ===Crystal structure of laccase from Cerrena maxima at 1.9A resolution=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| Laccases are members of the blue multi-copper oxidase family that oxidize substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. Crystals of the laccase from Cerrena maxima have been obtained and X-ray data were collected to 1.9 A resolution using synchrotron radiation. A preliminary analysis shows that the enzyme has the typical laccase structure and several carbohydrate sites have been identified. The carbohydrate chains appear to be involved in stabilization of the intermolecular contacts in the crystal structure, thus promoting the formation of well ordered crystals of the enzyme. Here, the results of an X-ray crystallographic study on the laccase from the fungus Cerrena maxima are reported. Crystals that diffract well to a resolution of at least 1.9 A (R factor = 18.953%; R(free) = 23.835; r.m.s.d. bond lengths, 0.06 A; r.m.s.d. bond angles, 1.07 degrees) have been obtained despite the presence of glycan moieties. The overall spatial organization of C. maxima laccase and the structure of its copper-containing active centre have been determined by the molecular-replacement method using the laccase from Trametes versicolor (Piontek et al., 2002) as a structural template. In addition, four glycan-binding sites were identified and the 1.9 A X-ray data were used to determine the previously unknown primary structure of this protein. The identity (calculated from sequence alignment) between the C. maxima laccase and the T. versicolor laccase is about 87%. Tyr196 and Tyr372 show significant extra density at the ortho positions and this has been interpreted in terms of NO(2) substituents.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17012782}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17012782 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_17012782}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 36: |
Line 40: |
| [[Category: Purification]] | | [[Category: Purification]] |
| [[Category: X-ray analyse]] | | [[Category: X-ray analyse]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:54:09 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:01:56 2008'' |