Purification, crystallization and preliminary X-ray diffraction analysis of the Staphylococcus epidermidis extracellular serine protease Esp

被引：6

作者：

Vengadesan, Krishnan ^{[1
]}

Macon, Kevin ^{[2
]}

Sugumoto, Shinya ^{[3
]}

Mizunoe, Yoshimitsu ^{[3
]}

Iwase, Tadayuki ^{[3
]}

Narayana, Sthanam V. L. ^{[2
]}

机构：

[1] UNESCO Reg Ctr Biotechnol RCB, Gurgaon 122016, Haryana, India

[2] Univ Alabama Birmingham, Sch Optometry, Ctr Biophys Sci & Engn, Birmingham, AL 35294 USA

[3] Jikei Univ, Sch Med, Dept Bacteriol, Minato Ku, Tokyo 1058461, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷

关键词：

POLYSACCHARIDE INTERCELLULAR ADHESIN; BIOFILM FORMATION; MOLECULAR-CLONING; AUREUS; ENDOPEPTIDASE; EXPRESSION; VIRULENCE; ENZYME; STRAIN;

D O I：

10.1107/S1744309112047124

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Esp, an extracellular serine protease from Staphylococcus epidermidis, has been shown to inhibit S. aureus biofilm formation and nasal colonization. The full-length 27 kDa pro-Esp was purified and digested with thermolysin to obtain mature Esp. The mature Esp containing 216 residues crystallized in space group P2(1), with unit-cell parameters a = 39.5, b = 61.2, c = 42.5 angstrom, beta = 98.2 degrees and one molecule in the asymmetric unit, with an estimated solvent content of 42%. A diffraction data set has been collected to 1.8 angstrom resolution on a rotating-anode home-source facility.

引用

页码：49 / 52

页数：4

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