Related ArticlesNMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein.
J Mol Biol. 2000 Aug 25;301(4):1003-17
Authors: Sekerina E, Rahfeld JU, Müller J, Fanghänel J, Rascher C, Fischer G, Bayer P
The 131-amino acid residue parvulin-like human peptidyl-prolyl cis/trans isomerase (PPIase) hPar14 was shown to exhibit sequence similarity to the regulator enzyme for cell cycle transitions human hPin1, but specificity for catalyzing pSer(Thr)-Pro cis/trans isomerizations was lacking. To determine the solution structure of hPar14 the (1)H, (13)C, and (15)N chemical shifts of this protein have been assigned using heteronuclear two and three-dimensional NMR experiments on unlabeled and uniformly (15)N/(13)C-labeled recombinant protein isolated from Escherichia coli cells that overexpress the protein. The chemical shift assignments were used to interpret the NOE data, which resulted in a total of 1042 NOE restraints. The NOE restraints were used along with 71 dihedral angle restraints and 38 hydrogen bonding restraints to produce 50 low-energy structures. The hPar14 folds into a betaalpha(3)betaalphabeta(2) structure, and contains an unstructured 35-amino acid basic tail N-terminal to the catalytic core that replaces the WW domain of hPin1 homologs. The three-dimensional structures of hPar14 and the PPIase domain of human hPin1 reveal a high degree of conservation. The root-mean-square deviations of the mean atomic coordinates of the heavy atoms of the backbone between residues 38 to 45, 50 to 58, 64 to 70, 81 to 86, 115 to 119 and 122 to 128 of hPar14 were 0.81(+/-0.07) A. The hPar14 model structure provides insight into how this class of PPIases may select preferential secondary catalytic sites, and also allows identification of a putative DNA-binding motif in parvulin-like PPIases.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Proteins. 2011 Oct;79(10):2988-91
Authors: Aramini JM, Rossi P, Fischer M, Xiao R, Acton TB, Montelione GT
Abstract
Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri,...
nmrlearner
Journal club
0
09-10-2011 06:51 PM
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
J Biol Chem. 2011 May 3;
Authors: Shin J, Chakraborty G, Bharatham N, Kang C, Tochio N, Koshiba S, Kigawa T, Kim W, Kim KT, Yoon HS
Vaccinia-related kinase 1 (VRK1) is one of the mitotic kinases which play important roles in cell cycle, nuclear condensation and transcription regulation. Kinase...
nmrlearner
Journal club
0
05-06-2011 12:02 PM
[NMR paper] NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprot
NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprotease-like tertiary structure.
Related Articles NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprotease-like tertiary structure.
J Struct Funct Genomics. 2005;6(1):51-62
Authors: Penhoat CH, Li Z, Atreya HS, Kim S, Yee A, Xiao R, Murray D, Arrowsmith CH, Szyperski T
The 150-residue protein TM1509 is encoded in gene YF09_THEMA of Thermotoga maritima. TM1509 has so far no functional annotation and belongs to protein family...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] NMR solution structure of the archaebacterial chromosomal protein MC1 reveals a new p
NMR solution structure of the archaebacterial chromosomal protein MC1 reveals a new protein fold.
Related Articles NMR solution structure of the archaebacterial chromosomal protein MC1 reveals a new protein fold.
Biochemistry. 2004 Nov 30;43(47):14971-8
Authors: Paquet F, Culard F, Barbault F, Maurizot JC, Lancelot G
The three-dimensional structure of methanogen chromosomal protein 1 (MC1), a chromosomal protein extracted from the archaebacterium Methanosarcina sp. CHTI55, has been solved using (1)H NMR spectroscopy. The small basic protein...
nmrlearner
Journal club
0
11-24-2010 10:03 PM
[NMR paper] NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain
NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein.
Related Articles NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein.
J Mol Biol. 2002 May 10;318(4):1097-115
Authors: Vogtherr M, Jacobs DM, Parac TN, Maurer M, Pahl A, Saxena K, Rüterjans H, Griesinger C, Fiebig KM
We have solved the solution structure of the...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] NMR spectroscopy reveals the solution dimerization interface of p53 core domains boun
NMR spectroscopy reveals the solution dimerization interface of p53 core domains bound to their consensus DNA.
Related Articles NMR spectroscopy reveals the solution dimerization interface of p53 core domains bound to their consensus DNA.
J Biol Chem. 2001 Dec 28;276(52):49020-7
Authors: Klein C, Planker E, Diercks T, Kessler H, Künkele KP, Lang K, Hansen S, Schwaiger M
The p53 protein is a transcription factor that acts as the major tumor suppressor in mammals. The core DNA-binding domain is mutated in about 50% of all human tumors. The...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] 1H NMR structure of an antifungal gamma-thionin protein SIalpha1: similarity to scorp
1H NMR structure of an antifungal gamma-thionin protein SIalpha1: similarity to scorpion toxins.
Related Articles 1H NMR structure of an antifungal gamma-thionin protein SIalpha1: similarity to scorpion toxins.
Proteins. 1998 Aug 15;32(3):334-49
Authors: Bloch C, Patel SU, Baud F, Zvelebil MJ, Carr MD, Sadler PJ, Thornton JM
The three-dimensional structure of the Sorghum bicolor seed protein gamma-thionin SIalpha1 has been determined by 2D 1H nuclear magnetic resonance (NMR) spectroscopy. The secondary structure of this 47-residue antifungal...
NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans
Linear Mode
