Structural highlights
Function
CAT3_NEUCR Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity).
Publication Abstract from PubMed
Polymorphism is frequently observed from different crystallization conditions. In proteins, the effect on conformational variability is poorly documented, with only a few reported examples. Here, three polymorphic crystal structures determined for a large-subunit catalase, CAT-3 from Neurospora crassa, are reported. Two of them belonged to new space groups, P1 and P43212, and a third structure belonged to the same space group, P212121, as the previously deposited 2.3 A resolution structure (PDB entry 3ej6), but had a higher resolution (1.95 A). Comparisons between these polymorphic structures highlight the conformational stability of tetrameric CAT-3 and reveal a distortion in the tetrameric structure that has not previously been described.
Conformational stability and crystal packing: polymorphism in Neurospora crassa CAT-3.,Zarate-Romero A, Stojanoff V, Rojas-Trejo SP, Hansberg W, Rudino-Pinera E Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul 1;69(Pt 7):753-8. doi:, 10.1107/S1744309113013468. Epub 2013 Jun 27. PMID:23832201[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zarate-Romero A, Stojanoff V, Rojas-Trejo SP, Hansberg W, Rudino-Pinera E. Conformational stability and crystal packing: polymorphism in Neurospora crassa CAT-3. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul 1;69(Pt 7):753-8. doi:, 10.1107/S1744309113013468. Epub 2013 Jun 27. PMID:23832201 doi:10.1107/S1744309113013468
