2hn1

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(New page: 200px<br /><applet load="2hn1" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hn1, resolution 2.900&Aring;" /> '''Crystal structure o...)
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==Overview==
==Overview==
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We describe the CorA Mg(2+) transporter homologue from Thermotoga maritima, in complex with 12 divalent cations at 3.7 A resolution. One metal is, found near the universally conserved GMN motif, apparently stabilized, within the transmembrane region. This portion of the selectivity filter, might discriminate between the size and preferred coordination geometry of, hydrated substrates. CorA may further achieve specificity by requiring the, sequential dehydration of substrates along the length of its approximately, 55 A long pore. Ten metal sites identified within the cytoplasmic funnel, domain are linked to long extensions of the pore helices and regulate the, transport status of CorA. We have characterized this region as an, intrinsic divalent cation sensor and provide evidence that it functions as, a Mg(2+)-specific homeostatic molecular switch. A proteolytic protection, assay, biophysical data, and comparison to a soluble domain structure from, Archaeoglobus fulgidus have revealed the potential reaction coordinate for, this diverse family of transport proteins.
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We describe the CorA Mg(2+) transporter homologue from Thermotoga maritima in complex with 12 divalent cations at 3.7 A resolution. One metal is found near the universally conserved GMN motif, apparently stabilized within the transmembrane region. This portion of the selectivity filter might discriminate between the size and preferred coordination geometry of hydrated substrates. CorA may further achieve specificity by requiring the sequential dehydration of substrates along the length of its approximately 55 A long pore. Ten metal sites identified within the cytoplasmic funnel domain are linked to long extensions of the pore helices and regulate the transport status of CorA. We have characterized this region as an intrinsic divalent cation sensor and provide evidence that it functions as a Mg(2+)-specific homeostatic molecular switch. A proteolytic protection assay, biophysical data, and comparison to a soluble domain structure from Archaeoglobus fulgidus have revealed the potential reaction coordinate for this diverse family of transport proteins.
==About this Structure==
==About this Structure==
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[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Pai, E.F.]]
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[[Category: Pai, E F.]]
[[Category: Payandeh, J.]]
[[Category: Payandeh, J.]]
[[Category: CO]]
[[Category: CO]]
[[Category: integral membrane protein fragment; metal transporter protein; divalent cations]]
[[Category: integral membrane protein fragment; metal transporter protein; divalent cations]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:24:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:43:36 2008''

Revision as of 15:43, 21 February 2008


2hn1, resolution 2.900Å

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Crystal structure of a CorA soluble domain from A. fulgidus in complex with Co2+

Overview

We describe the CorA Mg(2+) transporter homologue from Thermotoga maritima in complex with 12 divalent cations at 3.7 A resolution. One metal is found near the universally conserved GMN motif, apparently stabilized within the transmembrane region. This portion of the selectivity filter might discriminate between the size and preferred coordination geometry of hydrated substrates. CorA may further achieve specificity by requiring the sequential dehydration of substrates along the length of its approximately 55 A long pore. Ten metal sites identified within the cytoplasmic funnel domain are linked to long extensions of the pore helices and regulate the transport status of CorA. We have characterized this region as an intrinsic divalent cation sensor and provide evidence that it functions as a Mg(2+)-specific homeostatic molecular switch. A proteolytic protection assay, biophysical data, and comparison to a soluble domain structure from Archaeoglobus fulgidus have revealed the potential reaction coordinate for this diverse family of transport proteins.

About this Structure

2HN1 is a Single protein structure of sequence from Archaeoglobus fulgidus with as ligand. Full crystallographic information is available from OCA.

Reference

A structural basis for Mg2+ homeostasis and the CorA translocation cycle., Payandeh J, Pai EF, EMBO J. 2006 Aug 23;25(16):3762-73. Epub 2006 Aug 10. PMID:16902408

Page seeded by OCA on Thu Feb 21 17:43:36 2008

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