1gvc

From Proteopedia

Revision as of 11:23, 30 October 2007

18KDA N-II DOMAIN FRAGMENT OF DUCK OVOTRANSFERRIN + NTA

Overview

In a previous paper [Lindley et al. (1993), Acta Cryst. D49, 292-304], the, X-ray structure analysis of the 18 kDa fragment of duck ovotransferrin, corresponding to the NII domain of the intact protein, was reported at a, resolution of 2.3 A. In this structure, the Fe(III) cation binds to two, tyrosine residues and the synergistic carbonate anion in an identical, manner to that found in the intact protein. However, the aspartate and, histidine residues, normally involved in iron binding in transferrins, are, absent in the fragment and it was not possible to unequivocally define, what had replaced them. The electron density was tentatively assigned to, be a mixture of peptides, presumably resulting from the proteolytic, preparation of the fragment, binding to the iron through their amino ... [(full description)]

About this Structure

1GVC is a [Single protein] structure of sequence from [Anas platyrhynchos] with CO3, FE and NTA as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The mechanism of iron uptake by transferrins: the X-ray structures of the 18 kDa NII domain fragment of duck ovotransferrin and its nitrilotriacetate complex., Kuser P, Hall DR, Haw ML, Neu M, Evans RW, Lindley PF, Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):777-83. Epub 2002, Apr 26. PMID:11976488

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