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PMID: 12060744 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Crystal structure of conserved hypothetical protein Aq1575 from Aquifex aeolicus.

Shin DH, Yokota H, Kim R, Kim SH

Abstract

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 A x 10 A x 20 A 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.

MeSH Terms
Amino Acid Sequence Bacteria/chemistry Bacterial Proteins/chemistry,metabolism Conserved Sequence Molecular Conformation Molecular Sequence Data Protein Conformation Protein Folding Protein Structure, Secondary
Chemicals
Bacterial Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Shin Dong Hae
Department of Chemistry, University of California, Berkeley, CA 94720-5230, USA.
Yokota Hisao
Kim Rosalind
Kim Sung-Hou
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
2002-06-11
Pages
7980-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC123006
Subset
IM
Grants
NIGMS NIH HHS · P50 GM062412 · United States
NIGMS NIH HHS · GM 62412 · United States
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