Crystal Structure of Hypothetical Protein HP0062 (O24902_HELPY) from Helicobacter pylori at 1.65 Å Resolution

被引:7
作者
Jang, Sun-Bok [1 ]
Kwon, Ae-Ran [2 ]
Son, Woo-Sung [1 ]
Park, Sung Jean [1 ]
Lee, Bong-Jin [1 ]
机构
[1] Seoul Natl Univ, Coll Pharm, Res Inst Pharmaceut Sci, Seoul 151742, South Korea
[2] Daegu Haany Univ, Coll Herbal Bioind, Dept Herbal Skin Care, Gyongsan 712715, Gyeongsangbuk, South Korea
关键词
dimerization interface; Helicobacter pylori; helix-hairpin-helix structure; HP0062; leucine-zipper; COMPLETE GENOME SEQUENCE; EXPORT CHAPERONES; SECRETION SYSTEM; COILED COILS; III EXPORT; VIRULENCE; REFINEMENT; ALIGNMENT; GASTRITIS; ESXA;
D O I
10.1093/jb/mvp098
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 HP0062 gene encodes a small acidic protein of 86 amino acids with a theoretical pI of 4.6. The crystal structure of hypothetical protein HP0062 from Helicobacter pylori has been determined at 1.65 angstrom by molecular-replacement method. The crystallographic asymmetric unit contains dimer, in which HP0062 monomer folds into a helix-hairpin-helix structure. The two protomers are primarily held together by extensive hydrophobic interactions in an antiparallel arrangement, forming a four helix bundle. Aromatic residues located at a or g position in the heptad leucine zipper are not major contributor required for HP0062 dimerization but important for the thermostability of this protein.
引用
收藏
页码:535 / 540
页数:6
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