Comparative structural analysis of a histone-like protein from Spiroplasma melliferum in the crystalline state and in solution

被引：1

作者：

Gaponov, Yury A. ^{[1
]}

Timofeev, Vladimir I. ^{[1
,2
]}

Agapova, Yulia K. ^{[1
]}

Bocharov, Eduard V. ^{[3
]}

Shtykova, Eleonora V. ^{[2
]}

Rakitina, Tatiana V. ^{[1
,3
]}

机构：

[1] Kurchatov Inst, Natl Res Ctr, Moscow 123182, Russia

[2] Russian Acad Sci, A V Shubnikov Inst Crystallog, FSRC Crystallog & Photon, Moscow 119333, Russia

[3] Russian Acad Sci, M M Shemyakin Yu A Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia

来源：

MENDELEEV COMMUNICATIONS | 2022年 / 32卷 / 06期

基金：

俄罗斯基础研究基金会;

关键词：

small-angle X-ray scattering; SAXS; X-ray diffraction; XRD; nuclear magnetic resonance spectroscopy; NMR; crystal structure; structure in solution; histone-like HU protein; THERMAL-STABILITY;

D O I：

10.1016/j.mencom.2022.11.011

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A solution of a histone-like protein from Spiroplasma melliferum (HUSpm) was examined by small-angle X-ray scattering (SAXS). The experimental SAXS curve was compared with those calculated for the HUSpm structures from the PDB databank obtained by both X-ray diffraction analysis and nuclear magnetic resonance spectroscopy. The model of the HUSpm structure in solution, which best agrees with the experimental SAXS data, has a shorter distance between the centers of mass of the HUSpm monomers compared to the crystal structure, indicating that the HUSpm monomers can be located closer to each other in solution than in the crystalline state.

引用

页码：742 / 744

页数：3

共 20 条

[1] Structure-based inhibitors targeting the alpha-helical domain of the Spiroplasma melliferum histone-like HU protein [J].

Agapova, Yuliya K. ;

Altukhov, Dmitry A. ;

Timofeev, Vladimir I. ;

Stroylov, Victor S. ;

Mityanov, Vitaly S. ;

Korzhenevskiy, Dmitry A. ;

Vlaskina, Anna V. ;

Smirnova, Eugenia V. ;

Bocharov, Eduard V. ;

Rakitina, Tatiana V. .

SCIENTIFIC REPORTS, 2020, 10 (01)

[2] Structure and dynamics of a nanodisc by integrating NMR, SAXS and SANS experiments with molecular dynamics simulations [J].

Bengtsen, Tone ;

Holm, Viktor L. ;

Kjolbye, Lisbeth Ravnkilde ;

Midtgaard, Soren R. ;

Johansen, Nicolai Tidemand ;

Tesei, Giulio ;

Bottaro, Sandro ;

Schiott, Birgit ;

Arleth, Lise ;

Lindorff-Larsen, Kresten .

ELIFE, 2020, 9 :1-24

[3] Targeting Mycobacterium tuberculosis nucleoid-associated protein HU with structure-based inhibitors [J].

Bhowmick, Tuhin ;

Ghosh, Soumitra ;

Dixit, Karuna ;

Ganesan, Varsha ;

Ramagopal, Udupi A. ;

Dey, Debayan ;

Sarma, Siddhartha P. ;

Ramakumar, Suryanarayanarao ;

Nagaraja, Valakunja .

NATURE COMMUNICATIONS, 2014, 5

[4] Versatile sample environments and automation for biological solution X-ray scattering experiments at the P12 beamline (PETRA III, DESY) [J].

Blanchet, Clement E. ;

Spilotros, Alessandro ;

Schwemmer, Frank ;

Graewert, Melissa A. ;

Kikhney, Alexey ;

Jeffries, Cy M. ;

Franke, Daniel ;

Mark, Daniel ;

Zengerle, Roland ;

Cipriani, Florent ;

Fiedler, Stefan ;

Roessle, Manfred ;

Svergun, Dmitri I. .

JOURNAL OF APPLIED CRYSTALLOGRAPHY, 2015, 48 :431-443

[5] Structural basis of the high thermal stability of the histonelike HU protein from the mollicute Spiroplasma melliferum KC3 [J].

Boyko, Konstantin M. ;

Rakitina, Tatiana V. ;

Korzhenevskiy, Dmitry A. ;

Vlaskina, Anna V. ;

Agapova, Yuliya K. ;

Kamashev, Dmitry E. ;

Kleymenov, Sergey Y. ;

Popov, Vladimir O. .

SCIENTIFIC REPORTS, 2016, 6

[6] How to tackle protein structural data from solution and solid state: An integrated approach [J].

Carlon, Azzurra ;

Ravera, Enrico ;

Andralojc, Witold ;

Parigi, Giacomo ;

Murshudov, Garib N. ;

Luchinat, Claudio .

PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, 2016, 92-93 :54-70

[7] Chromosome organization in bacteria: mechanistic insights into genome structure and function [J].

Dame, Remus T. ;

Rashid, Fatema-Zahra M. ;

Grainger, David C. .

NATURE REVIEWS GENETICS, 2020, 21 (04) :227-242

[8]

Grove A, 2011, CURR ISSUES MOL BIOL, V13, P1

[9] Nucleoid Associated Proteins: The Small Organizers That Help to Cope With Stress [J].

Holowka, Joanna ;

Zakrzewska-Czerwinska, Jolanta .

FRONTIERS IN MICROBIOLOGY, 2020, 11

[10] Comparison of histone-like HU protein DNA-binding properties and HU/IHF protein sequence alignment [J].

Kamashev, Dmitri ;

Agapova, Yulia ;

Rastorguev, Sergey ;

Talyzina, Anna A. ;

Boyko, Konstantin M. ;

Korzhenevskiy, Dmitry A. ;

Vlaskina, Anna ;

Vasilov, Raif ;

Timofeev, Vladimir I. ;

Rakitina, Tatiana V. .

PLOS ONE, 2017, 12 (11)

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