Gast ::
| Hauptseite > Publikationsdatenbank > Conformational Fluctuations of UreG, an Intrinsically Disordered Enzyme > print |
| Hauptseite > Publikationsdatenbank > Conformational Fluctuations of UreG, an Intrinsically Disordered Enzyme > print |
| 001 | 201310 | ||
| 005 | 20240625095114.0 | ||
| 024 | 7 | _ | |2 doi |a 10.1021/bi4001744 |
| 024 | 7 | _ | |2 ISSN |a 0006-2960 |
| 024 | 7 | _ | |2 ISSN |a 1520-4995 |
| 024 | 7 | _ | |2 WOS |a WOS:000318333100010 |
| 037 | _ | _ | |a FZJ-2015-03615 |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Musiani, Francesco |b 0 |
| 245 | _ | _ | |a Conformational Fluctuations of UreG, an Intrinsically Disordered Enzyme |
| 260 | _ | _ | |a Columbus, Ohio |b American Chemical Society |c 2013 |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1433940074_12152 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 520 | _ | _ | |a UreG proteins are small GTP binding (G) proteins that catalyze the hydrolysis of GTP necessary for the maturation of urease, a virulence factor in bacterial pathogenesis. UreG proteins are the first documented cases of intrinsically disordered enzymes. The comprehension of the dynamics of folding−unfolding events occurring in this protein could shed light on the enzymatic mechanism of UreG. Here, we used the recently developed replica exchange with solute tempering (REST2) computational methodology to explore the conformational space of UreG from Helicobacter pylori (HpUreG) and to identify its structural fluctuations. The same simulation and analysis protocol has been applied to HypB from Methanocaldococcus jannaschii (MjHypB), which is closely related to UreG in both sequence and function, even though it is not intrinsically disordered. A comparison of the two systems reveals that both HpUreG and MjHypB feature a substantial rigidity of the protein regions involved in catalysis, justifying its residual catalytic activity. On the other hand, HpUreG tends to unfold more than MjHypB in portions involved in protein−protein interactions with metallochaperones necessary for the formation of multiprotein complexes known to be involved in urease activation. |
| 536 | _ | _ | |0 G:(DE-HGF)POF2-899 |a 899 - ohne Topic (POF2-899) |c POF2-899 |x 0 |f POF I |
| 588 | _ | _ | |a Dataset connected to CrossRef, juser.fz-juelich.de |
| 700 | 1 | _ | |0 P:(DE-Juel1)146009 |a Ippoliti, Emiliano |b 1 |u fzj |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Micheletti, Cristian |b 2 |
| 700 | 1 | _ | |0 P:(DE-Juel1)145614 |a Carloni, Paolo |b 3 |e Corresponding Author |u fzj |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Ciurli, Stefano |b 4 |e Corresponding Author |
| 773 | _ | _ | |0 PERI:(DE-600)1472258-6 |a 10.1021/bi4001744 |g Vol. 52, no. 17, p. 2949 - 2954 |n 17 |p 2949 - 2954 |t Biochemistry |v 52 |x 1520-4995 |y 2013 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/201310/files/bi4001744.pdf |y Restricted |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/201310/files/bi4001744.gif?subformat=icon |x icon |y Restricted |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/201310/files/bi4001744.jpg?subformat=icon-1440 |x icon-1440 |y Restricted |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/201310/files/bi4001744.jpg?subformat=icon-180 |x icon-180 |y Restricted |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/201310/files/bi4001744.jpg?subformat=icon-640 |x icon-640 |y Restricted |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/201310/files/bi4001744.pdf?subformat=pdfa |x pdfa |y Restricted |
| 909 | C | O | |o oai:juser.fz-juelich.de:201310 |p VDB |
| 910 | 1 | _ | |0 I:(DE-588b)1026307295 |6 P:(DE-HGF)0 |a German Research School for Simulation Sciences |b 0 |k GRS |
| 910 | 1 | _ | |0 I:(DE-588b)5008462-8 |6 P:(DE-Juel1)146009 |a Forschungszentrum Jülich GmbH |b 1 |k FZJ |
| 910 | 1 | _ | |0 I:(DE-588b)5008462-8 |6 P:(DE-Juel1)145614 |a Forschungszentrum Jülich GmbH |b 3 |k FZJ |
| 913 | 2 | _ | |0 G:(DE-HGF)POF3-899 |1 G:(DE-HGF)POF3-890 |2 G:(DE-HGF)POF3-800 |a DE-HGF |b Forschungsbereich Materie |l Forschungsbereich Materie |v ohne Topic |x 0 |
| 913 | 1 | _ | |0 G:(DE-HGF)POF2-899 |1 G:(DE-HGF)POF2-890 |2 G:(DE-HGF)POF2-800 |a DE-HGF |b Programmungebundene Forschung |l ohne Programm |v ohne Topic |x 0 |4 G:(DE-HGF)POF |3 G:(DE-HGF)POF2 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0100 |2 StatID |a JCR |
| 915 | _ | _ | |0 StatID:(DE-HGF)0110 |2 StatID |a WoS |b Science Citation Index |
| 915 | _ | _ | |0 StatID:(DE-HGF)0111 |2 StatID |a WoS |b Science Citation Index Expanded |
| 915 | _ | _ | |0 StatID:(DE-HGF)0150 |2 StatID |a DBCoverage |b Web of Science Core Collection |
| 915 | _ | _ | |0 StatID:(DE-HGF)0199 |2 StatID |a DBCoverage |b Thomson Reuters Master Journal List |
| 915 | _ | _ | |0 StatID:(DE-HGF)0200 |2 StatID |a DBCoverage |b SCOPUS |
| 915 | _ | _ | |0 StatID:(DE-HGF)0300 |2 StatID |a DBCoverage |b Medline |
| 915 | _ | _ | |0 StatID:(DE-HGF)0310 |2 StatID |a DBCoverage |b NCBI Molecular Biology Database |
| 915 | _ | _ | |0 StatID:(DE-HGF)1030 |2 StatID |a DBCoverage |b Current Contents - Life Sciences |
| 915 | _ | _ | |0 StatID:(DE-HGF)1050 |2 StatID |a DBCoverage |b BIOSIS Previews |
| 915 | _ | _ | |0 StatID:(DE-HGF)9900 |2 StatID |a IF < 5 |
| 920 | _ | _ | |l yes |
| 920 | 1 | _ | |0 I:(DE-Juel1)GRS-20100316 |k GRS |l GRS |x 0 |
| 920 | 1 | _ | |0 I:(DE-Juel1)IAS-5-20120330 |k IAS-5 |l Computational Biomedicine |x 1 |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a I:(DE-Juel1)GRS-20100316 |
| 980 | _ | _ | |a I:(DE-Juel1)IAS-5-20120330 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)INM-9-20140121 |
| 981 | _ | _ | |a I:(DE-Juel1)IAS-5-20120330 |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|