The 2.2 Å resolution structure of the catalase-peroxidase KatG from Synechococcus elongatus PCC7942

被引：5

作者：

Kamachi, Saori ^{[1
]}

Wada, Kei ^{[2
]}

Tamoi, Masahiro ^{[3
]}

Shigeoka, Shigeru ^{[3
]}

Tada, Toshiji ^{[1
]}

机构：

[1] Osaka Prefecture Univ, Grad Sch Sci, Sakai, Osaka 5998531, Japan

[2] Miyazaki Univ, Org Promot Tenure Track, Miyazaki 8891692, Japan

[3] Kinki Univ, Fac Agr, Nara 6318505, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷

关键词：

MYCOBACTERIUM-TUBERCULOSIS KATG; X-RAY-DIFFRACTION; CRYSTAL-STRUCTURE; SYNECHOCYSTIS PCC6803; PSEUDOMALLEI; REFINEMENT; MUTATIONS; LIGNIN; ADDUCT; SITE;

D O I：

10.1107/S2053230X14002052

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of catalase-peroxidase from Synechococcus elongatus PCC7942 (SeKatG) was solved by molecular replacement and refined to an R-work of 16.8% and an R-free of 20.6% at 2.2 angstrom resolution. The asymmetric unit consisted of only one subunit of the catalase-peroxidase molecule, including a protoporphyrin IX haem moiety and two sodium ions. A typical KatG covalent adduct was formed, Met248-Tyr222-Trp94, which is a key structural element for catalase activity. The crystallographic equivalent subunit was created by a twofold symmetry operation to form the functional dimer. The overall structure of the dimer was quite similar to other KatGs. One sodium ion was located close to the proximal Trp314. The location and configuration of the proximal cation site were very similar to those of typical peroxidases such as ascorbate peroxidase. These features may provide a structural basis for the behaviour of the radical localization/ delocalization during the course of the enzymatic reaction.

引用

页码：288 / 293

页数：6

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