Crystal structure of the tandem-type universal stress protein TTHA0350 from Thermus thermophilus HB8

被引:7
作者
Iino, Hitoshi [1 ,2 ]
Shimizu, Nobutaka [3 ]
Goto, Masaru [1 ,4 ]
Ebihara, Akio [1 ]
Fukui, Kenji [1 ]
Hirotsu, Ken [1 ]
Kuramitsu, Seiki [1 ,2 ]
机构
[1] RIKEN SPring 8 Ctr, Harima Inst, Sayo, Hyogo 6795148, Japan
[2] Osaka Univ, Grad Sch Sci, Dept Biol Sci, Osaka 5600043, Japan
[3] Japan Synchrotron Radiat Res Inst, Res & Utilizat Div, Sayo, Hyogo 6795198, Japan
[4] Toho Univ, Fac Sci, Dept Biomol Sci, Chiba 2748510, Japan
关键词
pfam00582; structural genomics; thermophile; TTHA0350; universal stress protein; BINDING; PROGRAM;
D O I
10.1093/jb/mvr057
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
The genome sequence of an extremely thermophilic bacterium, Thermus thermophilus HB8, revealed that TTHA0350 is a tandem-type universal stress protein (Usp) consisting of two Usp domains. Usp proteins, which are characterized by a conserved domain consisting of 130-160 amino acids, are inducibly expressed under a large number of stress conditions. The N-terminal domain of TTHA0350 contains a motif similar to the consensus ATP-binding one (G-2 x-G-9x-G-(S/T)), but the C-terminal one seems to lack the consensus motif. In order to determine its structural properties, we determined the crystal structures of TTHA0350 in the unliganded form and TTHA0350 center dot 2ATP at 2.50 and 1.70 A resolution, respectively. This is the first structure determination of a Usp family protein in both unliganded and ATP-liganded forms. TTHA0350 is folded into a fan-shaped structure which is similar to that of tandem-type Usp protein Rv2623 from Mycobacterium tuberculosis. However, the dimer assembly with C2-symmetry in TTHA0350 is quite different from that with D2-symmetry in Rv2623. The X-ray structure showed that not only the N-terminal but also the C-terminal domain binds one ATP, although the ATP-binding motif could not be detected in the C-terminal domain. The loop interacting with ATP in the C-terminal domain is in a conformation quite different from that in the N-terminal domain.
引用
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页码:295 / 302
页数:8
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