Solution structure of the highly acidic protein HI1450 from Haemophilus influenzae, a putative double‐stranded DNA mimic

• DOI: 10.1002/prot.10607
• Publication Date: 2004-01-23T13:00:32Z
• Authors: Lisa M. Parsons; Deok Cheon Yeh; John Orban
• Keywords: Yersinia pestis; Uracil-DNA glycosylase

Abstract The solution structure of the acidic protein HI1450 from Haemophilus influenzae has been determined by NMR spectroscopy. homologues in ten other bacterial species including Escherichia coli , Vibrio cholerae and Yersinia pestis but there are no functional assignments for any members family. Thirty‐one amino acids this 107‐residue aspartates or glutamates, contributing to an unusually low pI 3.72. secondary elements arranged α‐α‐β‐β‐β‐β order with two alpha helices packed against same side anti‐parallel four‐stranded beta meander. Two large loops, one between β1 β2 β3 bend almost perpendicularly across β‐strands opposite directions on non‐helical β‐sheet form a conserved hydrophobic cavity. some similarities double‐stranded DNA (dsDNA) mimic uracil glycosylase inhibitor (Ugi) distribution surface charges position Based these similarities, as well having comparable molecular dsDNA, we propose that may function dsDNA inhibit regulate yet unidentified binding protein. Proteins 2004;54:000–000. © 2003 Wiley‐Liss, Inc.