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The structure and evolution of the murine inhibitor of carbonic anhydrase: a member of the transferrin superfamily.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mason, Anne B. Eckenroth, Brian E. Lambert, Lisa A. Everse, Stephen J. McDevitt, Meghan E.
Description	Country affiliation: United States Author Affiliation: Eckenroth BE ( Department of Biochemistry, University of Vermont, Burlington, Vermont 05405, USA.)
Abstract	The original signature of the transferrin (TF) family of proteins was the ability to bind ferric iron with high affinity in the cleft of each of two homologous lobes. However, in recent years, new family members that do not bind iron have been discovered. One new member is the inhibitor of carbonic anhydrase (ICA), which as its name indicates, binds to and strongly inhibits certain isoforms of carbonic anhydrase. Recently, mouse ICA has been expressed as a recombinant protein in a mammalian cell system. Here, we describe the 2.4 Å structure of mouse ICA from a pseudomerohedral twinned crystal. As predicted, the structure is bilobal, comprised of two -ß domains per lobe typical of the other family members. As with all but insect TFs, the structure includes the unusual reverse Î³-turn in each lobe. The structure is consistent with the fact that introduction of two mutations in the N-lobe of murine ICA (mICA) (W124R and S188Y) allowed it to bind iron with high affinity. Unexpectedly, both lobes of the mICA were found in the closed conformation usually associated with presence of iron in the cleft, and making the structure most similar to diferric pig TF. Two new ICA family members (guinea pig and horse) were identified from genomic sequences and used in evolutionary comparisons. Additionally, a comparison of selection pressure (dN/dS) on functional residues reveals some interesting insights into the evolution of the TF family including that the N-lobe of lactoferrin may be in the process of eliminating its iron binding function.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1002/pro.439
Journal	Protein Science
Issue Number	9
Volume Number	19
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2010-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Carbonic Anhydrase Inhibitors Chemistry Transferrin Amino Acids Metabolism Animals Anions Crystallography, X-ray Mice Phylogeny Protein Binding Protein Conformation Protein Structure, Tertiary Genetics Research Support, N.i.h., Extramural Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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