| Structural highlights6hiv is a 154 chain structure with sequence from [1] and Trybb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | |
| Gene: | Tb927.8.5200 (TRYBB), TbgDal_V5090 (TRYBB), TbgDal_XI1730 (TRYBB), Tb10.70.7650 (TRYBB), Tb927.6.2010 (TRYBB), TbgDal_VI3990 (TRYBB), Tb927.7.3460 (TRYBB), TbgDal_VI3710 (TRYBB), Tb927.7.6800 (TRYBB), Tb10.61.3110 (TRYBB), Tb10.6k15.3290 (TRYBB), Tb10.70.7960 (TRYBB), Tb11.01.2340 (TRYBB), TbgDal_VI2240 (TRYBB), TbgDal_X13360 (TRYBB), Tb11.01.7140 (TRYBB), Tb927.6.1440 (TRYBB), TbgDal_XI6240 (TRYBB), TbgDal_X19420 (TRYBB), Tb927.7.3430 (TRYBB), TbgDal_III2230 (TRYBB), Tb927.6.4080 (TRYBB), Tb09.160.2250 (TRYBB), TbgDal_V5660 (TRYBB), TbgDal_XI9190 (TRYBB), TbgDal_VIII1510 (TRYBB), Tb927.3.820 (TRYBB), Tb927.6.1700 (TRYBB), Tb927.3.5300 (TRYBB), Tb11.01.1215 (TRYBB), TbgDal_X13710 (TRYBB), Tb927.6.4580 (TRYBB), Tb09.160.5050 (TRYBB), Tb10.26.0585 (TRYBB), Tb11.01.6285 (TRYBB), Tb10.61.3115 (TRYBB), Tb10.61.3155 (TRYBB), Tb927.2.2590 (TRYBB), TEOVI_000790200 (TRYBB), TbgDal_X9770 (TRYBB), TbgDal_II2470 (TRYBB), TbgDal_VII3350 (TRYBB), Tb09.160.4750 (TRYBB), Tb927.5.1790 (TRYBB), Tb11.02.3180 (TRYBB), Tb927.3.5240 (TRYBB), Tb927.6.2080 (TRYBB), Tb10.70.3840 (TRYBB), Tb927.6.4930 (TRYBB), Tb927.8.4550 (TRYBB), TbgDal_XI11660 (TRYBB), Tb11.01.2920 (TRYBB), Tb927.7.3240 (TRYBB), MURF5 (TRYBB), Tb10.70.0530 (TRYBB), Tb927.6.4560 (TRYBB), Tb10.70.4850 (TRYBB), Tb10.389.0130 (TRYBB), Tb927.8.3110 (TRYBB), Tb927.5.4040 (TRYBB), Tb10.406.0510 (TRYBB), RPS12 (TRYBB), Tb927.8.1430 (TRYBB), TB927.1.1200 (TRYBB), Tb11.02.5670 (TRYBB), Tb09.211.2580 (TRYBB), Tb10.70.4220 (TRYBB), Tb10.6k15.3900 (TRYBB), Tb927.6.2180 (TRYBB), Tb927.3.4130 (TRYBB), TbgDal_VII1040 (TRYBB), Tb09.211.2430 (TRYBB), Tb927.5.1510 (TRYBB), Tb09.211.3000 (TRYBB), Tb927.6.1250 (TRYBB), Tb927.3.770 (TRYBB), Tb927.8.5280 (TRYBB), TbgDal_VII2960 (TRYBB), Tb11.47.0024 (TRYBB), Tb10.70.6600 (TRYBB), Tb927.7.630 (TRYBB), Tb10.26.0750 (TRYBB), TEOVI_000558800 (TRYBB), Tb927.4.3690 (TRYBB), Tb11.01.1910 (TRYBB), Tb09.211.4510 (TRYBB), TEOVI_000532300 (TRYBB), Tb927.6.4040 (TRYBB), Tb09.160.5240 (TRYBB), TbgDal_IX4520 (TRYBB), Tb10.6k15.1920 (TRYBB), Tb927.4.2330 (TRYBB), Tb11.01.3300 (TRYBB), Tb927.4.1810 (TRYBB), TbgDal_X2260 (TRYBB), TbgDal_IV4820 (TRYBB), Tb927.3.5610 (TRYBB), TEOVI_000582800 (TRYBB), Tb927.5.3410 (TRYBB), TbgDal_V3970 (TRYBB), Tb927.2.4740, Tb927.2.4890 (TRYBB), Tb927.4.1070 (TRYBB), Tb927.5.3980 (TRYBB), Tb09.160.3800 (TRYBB), Tb927.7.3960 (TRYBB), Tb927.8.5860 (TRYBB), TB927.1.1210 (TRYBB), Tb11.01.1930 (TRYBB), TbgDal_VII4650 (TRYBB), TbgDal_VII3160 (TRYBB), Tb11.03.0260 (TRYBB), TbgDal_III1550 (TRYBB), Tb11.01.6620 (TRYBB), TbgDal_X14530 (TRYBB), Tb11.01.5460 (TRYBB), TbgDal_XI11060 (TRYBB), Tb11.01.1840 (TRYBB), Tb927.4.4600 (TRYBB), TbgDal_VII5370 (TRYBB), Tb927.5.3110 (TRYBB), Tb11.02.2250 (TRYBB), Tb927.7.2990, Tb927.7.3030 (TRYBB), TbgDal_VII8230 (TRYBB), Tb11.01.3500 (TRYBB) |
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 |
| Experimental data: | Check | | Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function[Q57WF8_TRYB2] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU363019] [Q383Y4_TRYB2] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU363019]
Publication Abstract from PubMed
Ribosomal RNA (rRNA) plays key functional and architectural roles in ribosomes. Using electron microscopy, we determined the atomic structure of a highly divergent ribosome found in mitochondria of Trypanosoma brucei, a unicellular parasite that causes sleeping sickness in humans. The trypanosomal mitoribosome features the smallest rRNAs and contains more proteins than all known ribosomes. The structure shows how the proteins have taken over the role of architectural scaffold from the rRNA: they form an autonomous outer shell that surrounds the entire particle and stabilizes and positions the functionally important regions of the rRNA. Our results also reveal the "minimal" set of conserved rRNA and protein components shared by all ribosomes that help us define the most essential functional elements.
Evolutionary shift toward protein-based architecture in trypanosomal mitochondrial ribosomes.,Ramrath DJF, Niemann M, Leibundgut M, Bieri P, Prange C, Horn EK, Leitner A, Boehringer D, Schneider A, Ban N Science. 2018 Sep 13. pii: science.aau7735. doi: 10.1126/science.aau7735. PMID:30213880[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See AlsoReferences
- ↑ Ramrath DJF, Niemann M, Leibundgut M, Bieri P, Prange C, Horn EK, Leitner A, Boehringer D, Schneider A, Ban N. Evolutionary shift toward protein-based architecture in trypanosomal mitochondrial ribosomes. Science. 2018 Sep 13. pii: science.aau7735. doi: 10.1126/science.aau7735. PMID:30213880 doi:http://dx.doi.org/10.1126/science.aau7735
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