Improving NMR Structures of RNA

被引:33
作者
Bermejo, Guillermo A. [1 ]
Clore, G. Marius [2 ]
Schwieters, Charles D. [1 ]
机构
[1] Natl Inst Hlth, Div Computat Biosci, Ctr Informat Technol, Bethesda, MD 20892 USA
[2] NIDDK, Phys Chem Lab, NIH, Bethesda, MD 20892 USA
关键词
CONFORMATIONAL DATABASE; STRUCTURE VALIDATION; ATOM CONTACTS; MEAN FORCE; XPLOR-NIH; REFINEMENT; POTENTIALS; PROTEINS; VISUALIZATION; MOLPROBITY;
D O I
10.1016/j.str.2016.03.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Here, we show that modern solution nuclear magnetic resonance (NMR) structures of RNA exhibit more steric clashes and conformational ambiguities than their crystallographic X-ray counterparts. To tackle these issues, we developed RNA-ff1, a new force field for structure calculation with Xplor-NIH. Using seven published NMR datasets, RNA-ff1 improves covalent geometry and MolProbity validation criteria for clashes and backbone conformation in most cases, relative to both the previous Xplor-NIH force field and the original structures associated with the experimental data. In addition, with smaller base-pair step rises in helical stems, RNA-ff1 structures enjoy more favorable base stacking. Finally, structural accuracy improves in the majority of cases, as supported by complete residual dipolar coupling cross-validation. Thus, the reported advances show great promise in bridging the quality gap that separates NMR and X-ray structures of RNA.
引用
收藏
页码:806 / 815
页数:10
相关论文
共 43 条
[1]   Smooth statistical torsion angle potential derived from a large conformational database via adaptive kernel density estimation improves the quality of NMR protein structures [J].
Bermejo, Guillermo A. ;
Clore, G. Marius ;
Schwieters, Charles D. .
PROTEIN SCIENCE, 2012, 21 (12) :1824-1836
[2]   A use of Ramachandran potentials in protein solution structure determinations [J].
Bertinia, I ;
Cavallaro, G ;
Luchinat, C ;
Poli, I .
JOURNAL OF BIOMOLECULAR NMR, 2003, 26 (04) :355-366
[3]   Crystallography & NMR system:: A new software suite for macromolecular structure determination [J].
Brunger, AT ;
Adams, PD ;
Clore, GM ;
DeLano, WL ;
Gros, P ;
Grosse-Kunstleve, RW ;
Jiang, JS ;
Kuszewski, J ;
Nilges, M ;
Pannu, NS ;
Read, RJ ;
Rice, LM ;
Simonson, T ;
Warren, GL .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 :905-921
[4]   MolProbity: all-atom structure validation for macromolecular crystallography [J].
Chen, Vincent B. ;
Arendall, W. Bryan, III ;
Headd, Jeffrey J. ;
Keedy, Daniel A. ;
Immormino, Robert M. ;
Kapral, Gary J. ;
Murray, Laura W. ;
Richardson, Jane S. ;
Richardson, David C. .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2010, 66 :12-21
[5]   R-factor, free R, and complete cross-validation for dipolar coupling refinement of NMR structures [J].
Clore, GM ;
Garrett, DS .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (39) :9008-9012
[6]   Improving the accuracy of NMR structures of RNA by means of conformational database potentials of mean force as assessed by complete dipolar coupling cross-validation [J].
Clore, GM ;
Kuszewski, J .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2003, 125 (06) :1518-1525
[7]   χ1 Rotamer populations and angles of mobile surface side chains are accurately predicted by a torsion angle database potential of mean force [J].
Clore, GM ;
Kuszewski, J .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (12) :2866-2867
[8]   MolProbity: all-atom contacts and structure validation for proteins and nucleic acids [J].
Davis, Ian W. ;
Leaver-Fay, Andrew ;
Chen, Vincent B. ;
Block, Jeremy N. ;
Kapral, Gary J. ;
Wang, Xueyi ;
Murray, Laura W. ;
Arendall, W. Bryan, III ;
Snoeyink, Jack ;
Richardson, Jane S. ;
Richardson, David C. .
NUCLEIC ACIDS RESEARCH, 2007, 35 :W375-W383
[9]   NMR structure of the A730 loop of the Neurospora VS ribozyme: insights into the formation of the active site [J].
Desjardins, Genevieve ;
Bonneau, Eric ;
Girard, Nicolas ;
Boisbouvier, Jerome ;
Legault, Pascale .
NUCLEIC ACIDS RESEARCH, 2011, 39 (10) :4427-4437
[10]   The structural stabilization of the κ three-way junction by Mg(II) represents the first step in the folding of a group II intron [J].
Donghi, Daniela ;
Pechlaner, Maria ;
Finazzo, Cinzia ;
Knobloch, Bernd ;
Sigel, Roland K. O. .
NUCLEIC ACIDS RESEARCH, 2013, 41 (04) :2489-2504