Structural highlights
3qpk is a 2 chain structure with sequence from Melao. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , |
| Related: | 1gw0, 2ih8, 2ih9, 2q9o, 3dkh, 3fu7, 3fu8, 3fu9, 3pps |
| Gene: | LAC1 (MELAO) |
| Activity: | Laccase, with EC number 1.10.3.2 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[LAC1_MELAO] Lignin degradation and detoxification of lignin-derived products (Probable).[1]
Publication Abstract from PubMed
Laccases catalyze the oxidation of phenolic substrates and the concominant reduction of dioxygen to water. We used xenon as an oxygen probe in search of routes for the entry of dioxygen into the catalytic center. Two xenon-pressurized crystal structures of recombinant Melanocarpus albomyces laccase were determined, showing three hydrophobic Xe-binding sites located in domain C. The analysis of hydrophobic cavities in other laccase structures further suggested the preference of domain C for binding of hydrophobic species such as dioxygen, thus suggesting that the hydrophobic core of domain C could function as a channel through which dioxygen can enter the trinuclear copper center.
Probing the Dioxygen Route in Melanocarpus albomyces Laccase with Pressurized Xenon Gas.,Kallio JP, Rouvinen J, Kruus K, Hakulinen N Biochemistry. 2011 May 5. PMID:21524088[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kiiskinen LL, Palonen H, Linder M, Viikari L, Kruus K. Laccase from Melanocarpus albomyces binds effectively to cellulose. FEBS Lett. 2004 Oct 8;576(1-2):251-5. PMID:15474046 doi:S0014579304010440
- ↑ Kallio JP, Rouvinen J, Kruus K, Hakulinen N. Probing the Dioxygen Route in Melanocarpus albomyces Laccase with Pressurized Xenon Gas. Biochemistry. 2011 May 5. PMID:21524088 doi:10.1021/bi200486b
