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Journal of Biochemistry Advance Access published online on June 29, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp098
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

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

Sun-Bok Jang1,{dagger}, Ae-Ran Kwon2,{dagger}, Woo-Sung Son1, Sung Jean Park1 and Bong-Jin Lee1,*

1Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, San 56-1, Shillim-Dong, Kwanak-Gu, Seoul 151-742, Korea
2 Department of Herbal Skin Care, College of Herbal Bio-Industry, Daegu Haany University, 290, Yugok-Dong, Gyeongsan-Si, Gyeongsangbuk-Do, 712-715, Korea

*To whom correspondence should be addressed: Prof. Bong-Jin Lee, Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, San 56-1, Shillim-Dong, Kwanak-Gu, Seoul 151-742, Korea Tel: 82-2-880-7869; Fax: 82-2-872-3632; E-mail: lbj{at}nmr.snu.ac.kr.

Received May 8, 2009; Accepted June 16, 2009


  Abstract

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 Å 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.

Key Words: Helicobacter pylori, HP0062, helix-hairpin-helix structure, leucine-zipper, dimerization interface

{dagger}Sun-Bok Jang and Ae-Ran Kwon contributed equally to this work.


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