Structure of the hypothetical protein TTHA1873 from Thermus thermophilus

被引：3

作者：

Yuvaraj, I ^{[1
]}

Chaudhary, Santosh Kumar ^{[1
]}

Jeyakanthan, J. ^{[2
]}

Sekar, K. ^{[1
]}

机构：

[1] Indian Inst Sci, Dept Computat & Data Sci, Bangalore 560012, Karnataka, India

[2] Alagappa Univ, Dept Bioinformat, Struct Biol & Bio Comp Lab, Karaikkudi 630004, Tamil Nadu, India

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2022年 / 78卷

关键词：

SAD phasing; hypothetical proteins; metalloproteins; jelly-roll topology; Thermus thermophilus; TTHA1873; calcium-binding proteins; ATOM-DATABASE-SYSTEM; CRYSTAL-STRUCTURE; SEQUENCE-ANALYSIS; CRYSTALLIZATION; ANNOTATION; SEARCH; TOOL;

D O I：

10.1107/S2053230X22008457

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of an uncharacterized hypothetical protein, TTHA1873 from Thermus thermophilus, has been determined by X-ray crystallography to a resolution of 1.78 angstrom using the single-wavelength anomalous dispersion method. The protein crystallized as a dimer in two space groups: P4(3)2(1)2 and P6(1)22. Structural analysis of the hypothetical protein revealed that the overall fold of TTHA1873 has a beta-sandwich jelly-roll topology with nine beta-strands. TTHA1873 is a dimeric metal-binding protein that binds to two Ca2+ ions per chain, with one on the surface and the other stabilizing the dimeric interface of the two chains. A structural homology search indicates that the protein has moderate structural similarity to one domain of cell-surface proteins or agglutinin receptor proteins. Red blood cells showed visible agglutination at high concentrations of the hypothetical protein.

引用

页码：338 / 346

页数：9

共 49 条

[21] The genome sequence of the extreme thermophile Thermus thermophilus [J].

Henne, A ;

Brüggemann, H ;

Raasch, C ;

Wiezer, A ;

Hartsch, T ;

Liesegang, H ;

Johann, A ;

Lienard, T ;

Gohl, O ;

Martinez-Arias, R ;

Jacobi, C ;

Starkuviene, V ;

Schlenczeck, S ;

Dencker, S ;

Huber, R ;

Klenk, HP ;

Kramer, W ;

Merkl, R ;

Gottschalk, G ;

Fritz, HJ .

NATURE BIOTECHNOLOGY, 2004, 22 (05) :547-553

[22] Dali server: conservation mapping in 3D [J].

Holm, Liisa ;

Rosenstrom, Paivi .

NUCLEIC ACIDS RESEARCH, 2010, 38 :W545-W549

[23] Annotation and curation of uncharacterized proteins- challenges [J].

Ijaq, Johny ;

Chandrasekharan, Mohanalatha ;

Poddar, Rajdeep ;

Bethi, Neeraja ;

Sundararajan, Vijayaraghava S. .

FRONTIERS IN GENETICS, 2015, 6

[24] PBEQ-Solver for online visualization of electrostatic potential of biomolecules [J].

Jo, Sunhwan ;

Vargyas, Miklos ;

Vasko-Szedlar, Judit ;

Roux, Benoit ;

Im, Wonpil .

NUCLEIC ACIDS RESEARCH, 2008, 36 :W270-W275

[25] MrBUMP: an automated pipeline for molecular replacement [J].

Keegan, Ronan M. ;

Winn, Martyn D. .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2008, 64 :119-124

[26] Stock-based detection of protein oligomeric states in js']jsPISA [J].

Krissinel, Eugene .

NUCLEIC ACIDS RESEARCH, 2015, 43 (W1) :W314-W319

[27] Factors enhancing protein thermostability [J].

Kumar, S ;

Tsai, CJ ;

Nussinov, R .

PROTEIN ENGINEERING, 2000, 13 (03) :179-191

[28] PROCHECK - A PROGRAM TO CHECK THE STEREOCHEMICAL QUALITY OF PROTEIN STRUCTURES [J].

LASKOWSKI, RA ;

MACARTHUR, MW ;

MOSS, DS ;

THORNTON, JM .

JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1993, 26 :283-291

[29] Solution structure of the hypothetical protein TA0095 from Thermoplasma acidophilum:: A novel superfamily with a two-layer sandwich architecture [J].

Leon, Esther ;

Yee, Adelinda ;

Ortiz, Angel R. ;

Santoro, Jorge ;

Rico, Manuel ;

Jimenez, M. Angeles .

PROTEIN SCIENCE, 2007, 16 (10) :2278-2286

[30] BALBES: a molecular-replacement pipeline [J].

Long, Fei ;

Vagin, Alexei A. ;

Young, Paul ;

Murshudov, Garib N. .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2008, 64 :125-132

← 1 2 3 4 5 →