000102168 001__ 102168
000102168 005__ 20230519145441.0
000102168 0247_ $$2doi$$a10.3390/ijms22063231
000102168 0248_ $$2sideral$$a124111
000102168 037__ $$aART-2021-124111
000102168 041__ $$aeng
000102168 100__ $$aNeira, J.L.
000102168 245__ $$aThe histidine phosphocarrier kinase/phosphorylase from bacillus subtilis is an oligomer in solution with a high thermal stability
000102168 260__ $$c2021
000102168 5060_ $$aAccess copy available to the general public$$fUnrestricted
000102168 5203_ $$aThe histidine phosphocarrier protein (HPr) kinase/phosphorylase (HPrK/P) modulates the phosphorylation state of the HPr protein, and it is involved in the use of carbon sources by Gram-positive bacteria. Its X-ray structure, as concluded from crystals of proteins from several species, is a hexamer; however, there are no studies about its conformational stability, and how its structure is modified by the pH. We have embarked on the conformational characterization of HPrK/P of Bacillus subtilis (bsHPrK/P) in solution by using several spectroscopic (namely, fluorescence and circular dichroism (CD)) and biophysical techniques (namely, small-angle X-ray-scattering (SAXS) and dynamic light-scattering (DLS)). bsHPrK/P was mainly a hexamer in solution at pH 7.0, in the presence of phosphate. The protein had a high conformational stability, with an apparent thermal denaturation midpoint of ~70¿ C, at pH 7.0, as monitored by fluorescence and CD. The protein was very pH-sensitive, precipitated between pH 3.5 and 6.5; below pH 3.5, it had a molten-globule-like conformation; and it acquired a native-like structure in a narrow pH range (between pH 7.0 and 8.0). Guanidinium hydrochloride (GdmCl) denaturation occurred through an oligomeric intermediate. On the other hand, urea denaturation occurred as a single transition, in the range of concentrations between 1.8 and 18 µM, as detected by far-UV CD and fluorescence.
000102168 536__ $$9info:eu-repo/grantAgreement/ES/AEI/CTQ2017-85425-P$$9info:eu-repo/grantAgreement/ES/MCIU-AEI-FEDER/RTI2018-097991-B-I00$$9info:eu-repo/grantAgreement/ES/MINECO/BIO2016-78020-R
000102168 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000102168 590__ $$a6.208$$b2021
000102168 592__ $$a1.176$$b2021
000102168 594__ $$a6.9$$b2021
000102168 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b69 / 297 = 0.232$$c2021$$dQ1$$eT1
000102168 593__ $$aComputer Science Applications$$c2021$$dQ1
000102168 591__ $$aCHEMISTRY, MULTIDISCIPLINARY$$b50 / 180 = 0.278$$c2021$$dQ2$$eT1
000102168 593__ $$aInorganic Chemistry$$c2021$$dQ1
000102168 593__ $$aSpectroscopy$$c2021$$dQ1
000102168 593__ $$aOrganic Chemistry$$c2021$$dQ1
000102168 593__ $$aPhysical and Theoretical Chemistry$$c2021$$dQ1
000102168 593__ $$aMolecular Biology$$c2021$$dQ1
000102168 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000102168 700__ $$aCámara-Artigas, A.
000102168 700__ $$aHernández-Cifre, J.G.
000102168 700__ $$aOrtore, M.G.
000102168 773__ $$g22, 6 (2021), 3231 [23 pp.]$$pInt. j. mol. sci.$$tInternational Journal of Molecular Sciences$$x1661-6596
000102168 8564_ $$s2219816$$uhttps://zaguan.unizar.es/record/102168/files/texto_completo.pdf$$yVersión publicada
000102168 8564_ $$s2692668$$uhttps://zaguan.unizar.es/record/102168/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000102168 909CO $$ooai:zaguan.unizar.es:102168$$particulos$$pdriver
000102168 951__ $$a2023-05-18-14:32:04
000102168 980__ $$aARTICLE