Structural highlights
1h58 is a 1 chain structure with sequence from Armru. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| Related: | 1atj, 1h55, 1h57, 1hch, 2atj, 3atj, 6atj, 7atj |
| Activity: | Peroxidase, with EC number 1.11.1.7 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[PER1A_ARMRU] Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions. Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time.
The catalytic pathway of horseradish peroxidase at high resolution.,Berglund GI, Carlsson GH, Smith AT, Szoke H, Henriksen A, Hajdu J Nature. 2002 May 23;417(6887):463-8. PMID:12024218[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Berglund GI, Carlsson GH, Smith AT, Szoke H, Henriksen A, Hajdu J. The catalytic pathway of horseradish peroxidase at high resolution. Nature. 2002 May 23;417(6887):463-8. PMID:12024218 doi:10.1038/417463a
