Crystal structure of exfoliative toxin D from Staphylococcus aureus

被引：1

作者：

Sato, Shu ^{[1
]}

Ragab, Rokaia F. ^{[2
]}

Guo, Xu ^{[2
]}

Elfadadny, Ahmed ^{[2
]}

Kozono, Takuma ^{[1
]}

Nishikawa, Atsushi ^{[1
]}

Nishifuji, Koji ^{[2
]}

Tonozuka, Takashi ^{[1
]}

机构：

[1] Tokyo Univ Agr & Technol, Dept Appl Biol Sci, Fuchu 1838509, Japan

[2] Tokyo Univ Agr & Technol, Grad Sch Agr, Div Anim Life Sci, Fuchu 1838509, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2024年 / 733卷

基金：

日本学术振兴会;

关键词：

Serine protease; Exfoliative toxin; Staphylococcus aureus; Crystal structure; Desmoglein-1; SUPERANTIGEN; SPECIFICITY; PROTEASE;

D O I：

10.1016/j.bbrc.2024.150689

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：

Staphylococcus aureus exfoliative toxins (ETs) are serine proteases responsible for staphylococcal scalded skin syndrome. Four ETs, ETA, ETB, ETD, and ETE, have been identified, all of which cleave desmoglein-1. This study presents the crystal structure of ETD at 1.75 & Aring; resolution. The protein exhibits a structure composed of two beta-barrels and two alpha-helices as described in previous studies of ETs. A predicted model of ETD in complex with Ile380-Glu381-Gly382-Pro383 (IEGP), a segment of human desmoglein-1 (hDsg1), was constructed. Glu381 of hDsg1 was predicted to interact with as many as six amino acid residues in ETD, whereas two amino acid residues in ETD primarily constituted subsite S1 ', and a space near subsite S1 ' was noted. It is likely that polypeptide chains located near the IEGP segment in the predicted structure of hDsg1 bind to this space. The structure of loop D, which was predicted to participate in subsite S2 ', in ETD was markedly different from those in other ETs.

引用

页数：5

共 27 条

[1] The CCP4 suite: integrative software for macromolecular crystallography [J].

Agirre, Jon ;

Atanasova, Mihaela ;

Bagdonas, Haroldas ;

Ballard, Charles B. ;

Basle, Arnaud ;

Beilsten-Edmands, James ;

Borges, Rafael J. ;

Brown, David G. ;

Burgos-Marmol, J. Javier ;

Berrisford, John M. ;

Bond, Paul S. ;

Caballero, Iracema ;

Catapano, Lucrezia ;

Chojnowski, Grzegorz ;

Cook, Atlanta G. ;

Cowtan, Kevin D. ;

Croll, Tristan I. ;

Debreczeni, Judit E. ;

Devenish, Nicholas E. ;

Dodson, Eleanor J. ;

Drevon, Tarik R. ;

Emsley, Paul ;

Evans, Gwyndaf ;

Evans, Phil R. ;

Fando, Maria ;

Foadi, James ;

Fuentes-Montero, Luis ;

Garman, Elspeth F. ;

Gerstel, Markus ;

Gildea, Richard J. ;

Hatti, Kaushik ;

Hekkelman, Maarten L. ;

Heuser, Philipp ;

Hoh, Soon Wen ;

Hough, Michael A. ;

Jenkins, Huw T. ;

Jimenez, Elisabet ;

Joosten, Robbie P. ;

Keegan, Ronan M. ;

Keep, Nicholas ;

Krissinel, Eugene B. ;

Kolenko, Petr ;

Kovalevskiy, Oleg ;

Lamzin, Victor S. ;

Lawson, David M. ;

Lebedev, Andrey A. ;

Leslie, Andrew G. W. ;

Lohkamp, Bernhard ;

Long, Fei ;

Maly, Martin .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2023, 79 :449-461

[2] Long-range Electrostatic Complementarity Governs Substrate Recognition by Human Chymotrypsin C, a Key Regulator of Digestive Enzyme Activation [J].

Batra, Jyotica ;

Szabo, Andras ;

Caulfield, Thomas R. ;

Soares, Alexei S. ;

Sahin-Toth, Miklos ;

Radisky, Evette S. .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2013, 288 (14) :9848-9859

[3] Exfoliative Toxins of Staphylococcus aureus [J].

Bukowski, Michal ;

Wladyka, Benedykt ;

Dubin, Grzegorz .

TOXINS, 2010, 2 (05) :1148-1165

[4] The structure of Staphylococcus aureus epidermolytic toxin A, an atypic serine protease, at 1.7 angstrom resolution [J].

Cavarelli, J ;

Prevost, G ;

Bourguet, W ;

Moulinier, L ;

Chevrier, B ;

Delagoutte, B ;

Bilwes, A ;

Mourey, L ;

Rifai, S ;

Piemont, Y ;

Moras, D .

STRUCTURE, 1997, 5 (06) :813-824

[5] An unusual helix-turn-helix protease inhibitory motif in a novel trypsin inhibitor from seeds of veronica (Veronica hederifolia L.) [J].

Conners, Rebecca ;

Konarev, Alexander V. ;

Forsyth, Jane ;

Lovegrove, Alison ;

Marsh, Justin ;

Joseph-Horne, Timothy ;

Shewry, Peter ;

Brady, R. Leo .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (38) :27760-27768

[6] AutoDock Vina 1.2.0: New Docking Methods, Expanded Force Field, and Python']Python Bindings [J].

Eberhardt, Jerome ;

Santos-Martins, Diogo ;

Tillack, Andreas F. ;

Forli, Stefano .

JOURNAL OF CHEMICAL INFORMATION AND MODELING, 2021, 61 (08) :3891-3898

[7] Features and development of Coot [J].

Emsley, P. ;

Lohkamp, B. ;

Scott, W. G. ;

Cowtan, K. .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2010, 66 :486-501

[8] How good are my data and what is the resolution? [J].

Evans, Philip R. ;

Murshudov, Garib N. .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2013, 69 :1204-1214

[9] Staphylococcus aureus Exfoliative Toxin E, Oligomeric State and Flip of P186: Implications for Its Action Mechanism [J].

Gismene, Carolina ;

Hernandez Gonzalez, Jorge Enrique ;

Nino Santisteban, Angela Rocio ;

Ziem Nascimento, Andrey Fabricio ;

Cunha, Lucas dos Santos ;

de Moraes, Fabio Rogerio ;

Pinto de Oliveira, Cristiano Luis ;

Oliveira, Caio C. ;

Scarin Provazzi, Paola Jocelan ;

Pascutti, Pedro Geraldo ;

Arni, Raghuvir Krishnaswamy ;

Mariutti, Ricardo Barros .

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2022, 23 (17)

[10] Enzymatic and molecular characteristics of the efficiency and specificity of exfoliative toxin cleavage of desmoglein 1 [J].

Hanakawa, Y ;

Schechter, NM ;

Lin, CY ;

Nishifuji, K ;

Amagai, M ;

Stanley, JR .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (07) :5268-5277

← 1 2 3 →