Lignin Peroxidase Crystal Structure Refined to 2.0 Angstroms
by T.L. Poulos / University of California, Irvine
Available on 1 platform
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Description
T.L. Poulos from the University of California, Irvine refined the crystal structure of the major lignin peroxidase isozyme from Phanerocheate chrysosporium. The model, refined to an R-factor of 0.15 for data between 8 and 2.03 Angstroms, includes 2 molecules per asymmetric unit, calcium ions, glucosamine modifications, and 476 water molecules. The refinement confirms earlier conclusions and details structural similarities and differences with cytochrome c peroxidase.
Use Cases
Comparative structural analysis based on the detailed atomic coordinates of lignin peroxidase.
Molecular dynamics simulations based on the refined model with water molecules and calcium ions.
Studying enzyme-substrate interactions based on the described heme pocket geometry and substrate binding site.
Protein engineering of peroxidases based on the noted structural differences with cytochrome c peroxidase.
Strengths
High-resolution refinement to 2.0 Angstroms with an R-factor of 0.15.
Excellent model geometry with a root mean square deviation from ideality in bond distances of 0.014 A and angles of 2.9 degrees.
Detailed structural comparison with cytochrome c peroxidase, including root mean square deviation metrics for backbone atoms (0.36 A) and alpha-carbons (2.65 A).
Limitations
Column-level documentation is absent; field semantics must be inferred after download.
Row count is unknown, which may limit suitability assessment.
Last update date is unknown; freshness unverified.