Structure of a Trypanosoma brucei α/β-hydrolase fold protein with unknown function

被引：5

作者：

Merritt, Ethan A. ^{[1
]}

Holmes, Margaret ^{[1
]}

Buckner, Frederick S. ^{[2
]}

Van Voorhis, Wesley C. ^{[2
]}

Quartly, Erin ^{[3
]}

Phizicky, Eric M. ^{[3
]}

Lauricella, Angela ^{[4
]}

Luft, Joseph ^{[4
]}

DeTitta, George ^{[4
]}

Neely, Helen ^{[1
]}

Zucker, Frank ^{[1
]}

Hol, Wim G. J. ^{[1
]}

机构：

[1] Univ Washington, Dept Biochem, Seattle, WA 98195 USA

[2] Univ Washington, Dept Med, Seattle, WA 98195 USA

[3] Univ Rochester, Sch Med, Dept Biochem & Biophys, Rochester, NY 14642 USA

[4] Hauptman Woodward Inst, Buffalo, NY 14203 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷

关键词：

D O I：

10.1107/S174430910801141X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The structure of a structural genomics target protein, Tbru020260AAA from Trypanosoma brucei, has been determined to a resolution of 2.2 angstrom using multiple-wavelength anomalous diffraction at the Se K edge. This protein belongs to Pfam sequence family PF08538 and is only distantly related to previously studied members of the alpha/beta-hydrolase fold family. Structural superposition onto representative alpha/beta-hydrolase fold proteins of known function indicates that a possible catalytic nucleophile, Ser116 in the T. brucei protein, lies at the expected location. However, the present structure and by extension the other trypanosomatid members of this sequence family have neither sequence nor structural similarity at the location of other active-site residues typical for proteins with this fold. Together with the presence of an additional domain between strands beta 6 and beta 7 that is conserved in trypanosomatid genomes, this suggests that the function of these homologs has diverged from other members of the fold family.

引用

页码：474 / 478

页数：5

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