Journal of Structural and Functional Genomics

, Volume 13, Issue 1, pp 27–36

Crystal structure of a putative isochorismatase hydrolase from Oleispira antarctica

Authors

  • Anna M. Goral
    • Department of Molecular Physiology and Biological PhysicsUniversity of Virginia
    • Midwest Center for Structural Genomics
    • Inter-Faculty Interdisciplinary Doctoral Studies in Natural Sciences and MathematicsUniversity of Warsaw
    • Faculty of ChemistryUniversity of Warsaw
  • Karolina L. Tkaczuk
    • Department of Molecular Physiology and Biological PhysicsUniversity of Virginia
    • Midwest Center for Structural Genomics
  • Maksymilian Chruszcz
    • Department of Molecular Physiology and Biological PhysicsUniversity of Virginia
    • Midwest Center for Structural Genomics
  • Olga Kagan
    • Banting and Best Department of Medical ResearchUniversity of Toronto
    • Midwest Center for Structural Genomics
  • Alexei Savchenko
    • Banting and Best Department of Medical ResearchUniversity of Toronto
    • Midwest Center for Structural Genomics
    • Department of Molecular Physiology and Biological PhysicsUniversity of Virginia
    • Midwest Center for Structural Genomics
Article

DOI: 10.1007/s10969-012-9127-5

Cite this article as:
Goral, A.M., Tkaczuk, K.L., Chruszcz, M. et al. J Struct Funct Genomics (2012) 13: 27. doi:10.1007/s10969-012-9127-5

Abstract

Isochorismatase-like hydrolases (IHL) constitute a large family of enzymes divided into five structural families (by SCOP). IHLs are crucial for siderophore-mediated ferric iron acquisition by cells. Knowledge of the structural characteristics of these molecules will enhance the understanding of the molecular basis of iron transport, and perhaps resolve which of the mechanisms previously proposed in the literature is the correct one. We determined the crystal structure of the apo-form of a putative isochorismatase hydrolase OaIHL (PDB code: 3LQY) from the antarctic γ-proteobacterium Oleispira antarctica, and did comparative sequential and structural analysis of its closest homologs. The characteristic features of all analyzed structures were identified and discussed. We also docked isochorismate to the determined crystal structure by in silico methods, to highlight the interactions of the active center with the substrate. The putative isochorismate hydrolase OaIHL from O. antarctica possesses the typical catalytic triad for IHL proteins. Its active center resembles those IHLs with a D–K–C catalytic triad, rather than those variants with a D–K–X triad. OaIHL shares some structural and sequential features with other members of the IHL superfamily. In silico docking results showed that despite small differences in active site composition, isochorismate binds to in the structure of OaIHL in a similar mode to its binding in phenazine biosynthesis protein PhzD (PDB code 1NF8).

Keywords

Iron uptakeIsochorismatase hydrolasesStructural comparison of isochorismatasesStructural genomics

Abbreviations

OaIHL

Putative isochorismatase hydrolase from Oleispira antarctica

IHL

Isochorismatase-like hydrolase

ISC

Isochorismate/isochorismic acid

Å

Angstrom

SCOP

Structural classification of proteins

PDB

Protein Data Bank

RMSD

Root mean square deviation

MSA

Multiple sequence alignment

Copyright information

© Springer Science+Business Media B.V. 2012