Structural highlights
3rzt is a 1 chain structure with sequence from Pyrfu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 3kyx, 3ryg, 3rz6, 3rzr |
| Gene: | PF1282, rub (PYRFU) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[RUBR_PYRFU] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
Publication Abstract from PubMed
Neutron crystallography is a powerful technique for experimental visualization of the positions of light atoms, including hydrogen and its isotope deuterium. In recent years, structural biologists have shown increasing interest in the technique as it uniquely complements X-ray crystallographic data by revealing the positions of D atoms in macromolecules. With this regained interest, access to macromolecular neutron crystallography beamlines is becoming a limiting step. In this report, it is shown that a rapid data-collection strategy can be a valuable alternative to longer data-collection times in appropriate cases. Comparison of perdeuterated rubredoxin structures refined against neutron data sets collected over hours and up to 5 d shows that rapid neutron data collection in just 14 h is sufficient to provide the positions of 269 D atoms without ambiguity.
Rapid visualization of hydrogen positions in protein neutron crystallographic structures.,Munshi P, Chung SL, Blakeley MP, Weiss KL, Myles DA, Meilleur F Acta Crystallogr D Biol Crystallogr. 2012 Jan;68(Pt 1):35-41. Epub 2011, Dec 9. PMID:22194331[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Munshi P, Chung SL, Blakeley MP, Weiss KL, Myles DA, Meilleur F. Rapid visualization of hydrogen positions in protein neutron crystallographic structures. Acta Crystallogr D Biol Crystallogr. 2012 Jan;68(Pt 1):35-41. Epub 2011, Dec 9. PMID:22194331 doi:10.1107/S0907444911048402
