Structural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold.

scientific article

Structural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1080/07391102.2017.1417162
P698PubMed publication ID29283021

P50authorVladimir TimofeevQ56480295
Tatiana V RakitinaQ89744995
P2093author name stringEduard V Bocharov
Sergey Yu Kleymenov
Yulia K Agapova
Dmitry A Altukhov
Anna A Talyzina
Dmitry A Korzhenevskiy
Anna V Vlaskina
P2860cites workAn overview of recent developments in the interpretation and prediction of fast internal protein dynamicsQ36846761
Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3.Q37390158
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The stability of the archaeal HU histone-like DNA-binding protein from Thermoplasma volcanium.Q38360496
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Complete 1H, 15N and 13C assignment of trappin-2 and 1H assignment of its two domains, elafin and cementoinQ39995853
Coordination of genomic structure and transcription by the main bacterial nucleoid-associated protein HU.Q42007285
Investigation of the structural basis for thermostability of DNA-binding protein HU from Bacillus stearothermophilusQ43025606
High-resolution X-ray structure of the DNA-binding protein HU from the hyper-thermophilic Thermotoga maritima and the determinants of its thermostabilityQ43032809
Mycoplasma gallisepticum produces a histone-like protein that recognizes base mismatches in DNA.Q45843019
Thermodynamic analysis of the unfolding and stability of the dimeric DNA-binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima and its E34D mutant.Q47813618
An alternate conformation of the hyperthermostable HU protein from Thermotoga maritima has unexpectedly high flexibility.Q47822230
Structural and evolutionary analyses reveal determinants of DNA binding specificities of nucleoid-associated proteins HU and IHF.Q51299285
Salt-dependent and protein-concentration-dependent changes in the solution structure of the DNA-binding histone-like protein, HBsu, from Bacillus subtilis.Q53026524
Essential genes of a minimal bacteriumQ22066349
A whole-cell computational model predicts phenotype from genotypeQ24622101
TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shiftsQ24651272
HU multimerization shift controls nucleoid compactionQ27333092
Flexible DNA bending in HU-DNA cocrystal structuresQ27641656
Spiral structure of Escherichia coli HU   provides foundation for DNA supercoilingQ27644063
Targeting Mycobacterium tuberculosis nucleoid-associated protein HU with structure-based inhibitorsQ27690716
HU histone-like DNA-binding protein from Thermus thermophilus: structural and evolutionary analysesQ27713604
Solution structure of the HU protein from Bacillus stearothermophilusQ27729327
VMD: visual molecular dynamicsQ27860554
Comparative protein modelling by satisfaction of spatial restraintsQ27860866
GROMACS: fast, flexible, and freeQ27860998
pi-Stacking interactions. Alive and well in proteinsQ28273506
Enhanced conformational flexibility of the histone-like (HU) protein from Mycoplasma gallisepticum.Q30395629
The HU regulon is composed of genes responding to anaerobiosis, acid stress, high osmolarity and SOS inductionQ33405760
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein from Spiroplasma melliferum KC3.Q35006982
IHF and HU: flexible architects of bent DNA.Q35753197
Crystal structure of histone-like protein from Streptococcus mutans refined to 1.9 Å resolution.Q36771604
P433issue16
P921main subjectSpiroplasma melliferumQ3966882
P304page(s)4392-4404
P577publication date2018-01-07
P1433published inJournal of Biomolecular Structure and DynamicsQ15754747
P1476titleStructural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold
P478volume36