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.
| Original language | English |
|---|---|
| Pages (from-to) | 535-540 |
| Number of pages | 6 |
| Journal | Journal of Biochemistry |
| Volume | 146 |
| Issue number | 4 |
| DOIs | |
| State | Published - Oct 2009 |
Bibliographical note
Funding Information:Ministry of Education, Science and Technology (MEST); Innovative Drug Research Center for Metabolic and Inflammatory Disease; 2008 BK21 Project for Medicine, Dentistry and Pharmacy; New Drug Target Discovery (grant number 370C-20070095).
Keywords
- Dimerization interface
- HP0062
- Helicobacter pylori
- Helix-hairpin-helix structure
- Leucine-zipper