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Crystal structure of the secreted protein HP1454 from the human pathogen Helicobacter pylori
Author(s) -
Quarantini Sandra,
Cendron Laura,
Zanotti Giuseppe
Publication year - 2014
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24608
Subject(s) - antiparallel (mathematics) , orthorhombic crystal system , crystallography , domain (mathematical analysis) , helix bundle , structural similarity , helix (gastropod) , helicobacter pylori , protein structure , crystal structure , biology , chemistry , physics , biochemistry , genetics , mathematics , mathematical analysis , ecology , quantum mechanics , snail , magnetic field
HP1454 is a protein of 303 amino acids found in the extracellular milieu of Helicobacter pylori . The protein structure, crystallized in the orthorhombic C222 1 space group with one molecule per asymmetric unit, has been determined using the single‐wavelength anomalous dispersion method. HP1454 exhibits an elongated bent shape, composed of three distinct domains. Each domain possesses a fold already present in other structures: Domain I contains a three‐strand antiparallel β‐barrel flanked by a long α‐helix, Domain II is an anti‐parallel three‐helix bundle, and Domain III a β‐sheet flanked by two α‐helices. The overall assembly of the protein does not bear any similarity with known structures. Proteins 2014; 82:2868–2873. © 2014 Wiley Periodicals, Inc.