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Crystallographic refinement of lignin peroxidase at 2 A.
Open accessAbstract
The crystal structure of the major lignin peroxidase isozyme from Phanerocheate chrysosporium has been Tefined to an R = 0.15 for data between 8 A and 2.03A. The refined model consists of 2 lignin peroxidase molecules in the asymmetric unit, 2 calcium ions per monomer, 1 glucosamine per monomer N-linked to Asn-257, and 476 water molecules per asymmetric unit.The model exhibits excellent geometry with a root mean square deviation fFom ideality in bond distances and angles of 0.014 A and 2.9", respectively.Molecule 1 consists of all 343 residues, while molecule 2 consists of residues 1-341.The overall root mean square deviation in backbone atoms bgtween the 2 molecules in the asymmetric unit is 0.36 A. The refinement at 2.0 A confirm! our conclusions based on the partially refined 2.
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Cited by
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Active site structure and catalytic mechanisms of human peroxidases
Furtmüller, P. G., Zederbauer, M., Jantschko, W., Helm, J., Bogner, M., Jakopitsch, C., & Obinger, C. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.09.017 · Cited by 358
Horseradish peroxidase: a valuable tool in biotechnology
Azevedo, A. M., Martins, V. C., Prazeres, D. M. F., Vojinović, V., Cabral, J. M. S., & Fonseca, L. P. (2003) · Biotechnology Annual Review · doi:10.1016/s1387-2656(03)09003-3 · Cited by 243
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Metadata
- Authors
- Poulos, T. L., Edwards, S. L., Wariishi, H., & Gold, M. H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-02
- Volume
- 268
- Issue
- 6
- Pages
- 4429-4440
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W4252948366
- Cited by
- 346
- References
- 0
- FWCI
- 26.28
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Poulos, T. L., Edwards, S. L., Wariishi, H., & Gold, M. H. (1993). Crystallographic refinement of lignin peroxidase at 2 A. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)53627-9
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