Crystal structure of conserved hypothetical protein Aq1575 from Aquifex aeolicus

Dong Hae Shin, Hisao Yokota, Rosalind Kim, Sung Hou Kim

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


The crystal structure of a conserved hypothetical protein, Aq1575, from Aquifex aeolicus has been determined by using x-ray crystallography. The protein belongs to the domain of unknown function DUF28 in the Pfam and PALI databases for which there was no structural information available until now. A structural homology search with the DALI algorithm indicates that this protein has a new fold with no obvious similarity to those of other proteins of known three-dimensional structure. The protein reveals a monomer consisting of three domains arranged along a pseudo threefold symmetry axis. There is a large cleft with approximate dimensions of 10 Å × 10 Å × 20 Å in the center of the three domains along the symmetry axis. Two possible active sites are suggested based on the structure and multiple sequence alignment. There are several highly conserved residues in these putative active sites. The structure based molecular properties and thermostability of the protein are discussed.

Original languageEnglish
Pages (from-to)7980-7985
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number12
StatePublished - 11 Jun 2002


  • DUF28
  • Hyperthermophile
  • New fold
  • Structural genomics
  • Thermostability


Dive into the research topics of 'Crystal structure of conserved hypothetical protein Aq1575 from Aquifex aeolicus'. Together they form a unique fingerprint.

Cite this