Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense

The crystal structure of a microbial transglutaminase from Streptoverticillium mobaraense has been determined at 2.4 A resolution. The protein folds into a plate-like shape, and has one deep cleft at the edge of the molecule. Its overall structure is completely different from that of the factor XIII...

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Bibliographic Details
Published in:The Journal of biological chemistry 2002-11, Vol.277 (46), p.44252-44260
Main Authors: Kashiwagi, Tatsuki, Yokoyama, Kei-Ichi, Ishikawa, Kohki, Ono, Kunio, Ejima, Daisuke, Matsui, Hiroshi, Suzuki, Ei-ichiro
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Aspartic Acid - chemistry
Binding Sites
Catalysis
Cross-Linking Reagents - pharmacology
Crystallography, X-Ray
Cysteine - chemistry
Escherichia coli - metabolism
Histidine - chemistry
Models, Chemical
Models, Molecular
Molecular Sequence Data
Protein Structure, Tertiary
Streptomyces - chemistry
Structure-Activity Relationship
Transglutaminases - chemistry
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Summary:The crystal structure of a microbial transglutaminase from Streptoverticillium mobaraense has been determined at 2.4 A resolution. The protein folds into a plate-like shape, and has one deep cleft at the edge of the molecule. Its overall structure is completely different from that of the factor XIII-like transglutaminase, which possesses a cysteine protease-like catalytic triad. The catalytic residue, Cys(64), exists at the bottom of the cleft. Asp(255) resides at the position nearest to Cys(64) and is also adjacent to His(274). Interestingly, Cys(64), Asp(255), and His(274) superimpose well on the catalytic triad "Cys-His-Asp" of the factor XIII-like transglutaminase, in this order. The secondary structure frameworks around these residues are also similar to each other. These results imply that both transglutaminases are related by convergent evolution; however, the microbial transglutaminase has developed a novel catalytic mechanism specialized for the cross-linking reaction. The structure accounts well for the catalytic mechanism, in which Asp(255) is considered to be enzymatically essential, as well as for the causes of the higher reaction rate, the broader substrate specificity, and the lower deamidation activity of this enzyme.
ISSN:0021-9258
DOI:10.1074/jbc.M203933200