1xvx

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(New page: 200px<br /><applet load="1xvx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xvx, resolution 1.53&Aring;" /> '''Crystal Structure of...)
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'''Crystal Structure of iron-loaded Yersinia enterocolitica YfuA'''<br />
'''Crystal Structure of iron-loaded Yersinia enterocolitica YfuA'''<br />
==Overview==
==Overview==
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The uptake of the element iron is vital for the survival of most, organisms. Numerous pathogenic Gram-negative bacteria utilize a, periplasm-to-cytosol ATP-binding cassette transport pathway to transport, this essential atom in to the cell. In this study, we investigated the, Yersinia enterocolitica (YfuA) and Serratia marcescens (SfuA) iron-binding, periplasmic proteins. We have determined the 1.8-angstroms structures of, iron-loaded (YfuA) and iron-free (SfuA) forms of this class of proteins., Although the sequence of these proteins varies considerably from the other, members of the transferrin structural superfamily, they adopt the same, three-dimensional fold. The iron-loaded YfuA structure illustrates the, unique nature of this new class of proteins in that they are able to, octahedrally coordinate the ferric ion in the absence of a bound anion., The iron-free SfuA structure contains a bound citrate anion in the, iron-binding cleft that tethers the N- and C-terminal domains of the apo, protein and stabilizes the partially open structure.
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The uptake of the element iron is vital for the survival of most organisms. Numerous pathogenic Gram-negative bacteria utilize a periplasm-to-cytosol ATP-binding cassette transport pathway to transport this essential atom in to the cell. In this study, we investigated the Yersinia enterocolitica (YfuA) and Serratia marcescens (SfuA) iron-binding periplasmic proteins. We have determined the 1.8-angstroms structures of iron-loaded (YfuA) and iron-free (SfuA) forms of this class of proteins. Although the sequence of these proteins varies considerably from the other members of the transferrin structural superfamily, they adopt the same three-dimensional fold. The iron-loaded YfuA structure illustrates the unique nature of this new class of proteins in that they are able to octahedrally coordinate the ferric ion in the absence of a bound anion. The iron-free SfuA structure contains a bound citrate anion in the iron-binding cleft that tethers the N- and C-terminal domains of the apo protein and stabilizes the partially open structure.
==About this Structure==
==About this Structure==
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1XVX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica] with FE, ZN, CO3 and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XVX OCA].
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1XVX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CO3:'>CO3</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XVX OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Yersinia enterocolitica]]
[[Category: Yersinia enterocolitica]]
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[[Category: Dougan, D.R.]]
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[[Category: Dougan, D R.]]
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[[Category: McRee, D.E.]]
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[[Category: McRee, D E.]]
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[[Category: Schryvers, A.B.]]
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[[Category: Schryvers, A B.]]
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[[Category: Shouldice, S.R.]]
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[[Category: Shouldice, S R.]]
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[[Category: Tari, L.W.]]
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[[Category: Tari, L W.]]
[[Category: CO3]]
[[Category: CO3]]
[[Category: EDO]]
[[Category: EDO]]
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[[Category: periplasmic iron binding protein]]
[[Category: periplasmic iron binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:02:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:59:14 2008''

Revision as of 13:59, 21 February 2008


1xvx, resolution 1.53Å

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Crystal Structure of iron-loaded Yersinia enterocolitica YfuA

Overview

The uptake of the element iron is vital for the survival of most organisms. Numerous pathogenic Gram-negative bacteria utilize a periplasm-to-cytosol ATP-binding cassette transport pathway to transport this essential atom in to the cell. In this study, we investigated the Yersinia enterocolitica (YfuA) and Serratia marcescens (SfuA) iron-binding periplasmic proteins. We have determined the 1.8-angstroms structures of iron-loaded (YfuA) and iron-free (SfuA) forms of this class of proteins. Although the sequence of these proteins varies considerably from the other members of the transferrin structural superfamily, they adopt the same three-dimensional fold. The iron-loaded YfuA structure illustrates the unique nature of this new class of proteins in that they are able to octahedrally coordinate the ferric ion in the absence of a bound anion. The iron-free SfuA structure contains a bound citrate anion in the iron-binding cleft that tethers the N- and C-terminal domains of the apo protein and stabilizes the partially open structure.

About this Structure

1XVX is a Single protein structure of sequence from Yersinia enterocolitica with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Novel anion-independent iron coordination by members of a third class of bacterial periplasmic ferric ion-binding proteins., Shouldice SR, McRee DE, Dougan DR, Tari LW, Schryvers AB, J Biol Chem. 2005 Feb 18;280(7):5820-7. Epub 2004 Dec 2. PMID:15576371

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