Structural highlights
5syk is a 2 chain structure with sequence from Burkholderia pseudomallei 1710b. This structure supersedes the now removed PDB entry 4mvp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 1.8Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
KATG_BURP1 Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Publication Abstract from PubMed
Catalase peroxidases (KatG's) are bifunctional heme proteins that can disproportionate hydrogen peroxide (catalatic reaction) despite their structural dissimilarity with monofunctional catalases. Using X-ray crystallography and QM/MM calculations, we demonstrate that the catalatic reaction of KatG's involves deprotonation of the active-site Trp, which plays a role similar to that of the distal His in monofunctional catalases. The interaction of a nearby mobile arginine with the distal Met-Tyr-Trp essential adduct (in/out) acts as an electronic switch, triggering deprotonation of the adduct Trp.
An ionizable active-site tryptophan imparts catalase activity to a peroxidase core.,Loewen PC, Carpena X, Vidossich P, Fita I, Rovira C J Am Chem Soc. 2014 May 21;136(20):7249-52. doi: 10.1021/ja502794e. Epub 2014 May, 7. PMID:24785434[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Loewen PC, Carpena X, Vidossich P, Fita I, Rovira C. An ionizable active-site tryptophan imparts catalase activity to a peroxidase core. J Am Chem Soc. 2014 May 21;136(20):7249-52. doi: 10.1021/ja502794e. Epub 2014 May, 7. PMID:24785434 doi:http://dx.doi.org/10.1021/ja502794e
