1d5t

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(New page: 200px<br /><applet load="1d5t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d5t, resolution 1.04&Aring;" /> '''GUANINE NUCLEOTIDE D...)
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[[Image:1d5t.jpg|left|200px]]<br /><applet load="1d5t" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1d5t, resolution 1.04&Aring;" />
caption="1d5t, resolution 1.04&Aring;" />
'''GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR, ALPHA-ISOFORM'''<br />
'''GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR, ALPHA-ISOFORM'''<br />
==Overview==
==Overview==
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Guanine nucleotide dissociation inhibitor (GDI) is a 55-kDa protein that, functions in vesicular membrane transport to recycle Rab GTPases. We have, now determined the crystal structure of bovine alpha-GDI at ultra-high, resolution (1.04 A). Refinement at this resolution highlighted a region, with high mobility of its main-chain residues. This corresponded to a, surface loop in the primarily alpha-helical domain II at the base of, alpha-GDI containing the previously uncharacterized sequence-conserved, region (SCR) 3A. Site-directed mutagenesis showed that this mobile loop, plays a crucial role in binding of GDI to membranes and extraction of, membrane-bound Rab. This domain, referred to as the mobile effector loop, in combination with Rab-binding residues found in the multi-sheet domain I, at the apex of alpha-GDI may provide flexibility for recycling of diverse, Rab GTPases. We propose that conserved residues in domains I and II, synergize to form the functional face of GDI, and that domain II mediates, a critical step in Rab recycling during vesicle fusion.
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Guanine nucleotide dissociation inhibitor (GDI) is a 55-kDa protein that functions in vesicular membrane transport to recycle Rab GTPases. We have now determined the crystal structure of bovine alpha-GDI at ultra-high resolution (1.04 A). Refinement at this resolution highlighted a region with high mobility of its main-chain residues. This corresponded to a surface loop in the primarily alpha-helical domain II at the base of alpha-GDI containing the previously uncharacterized sequence-conserved region (SCR) 3A. Site-directed mutagenesis showed that this mobile loop plays a crucial role in binding of GDI to membranes and extraction of membrane-bound Rab. This domain, referred to as the mobile effector loop, in combination with Rab-binding residues found in the multi-sheet domain I at the apex of alpha-GDI may provide flexibility for recycling of diverse Rab GTPases. We propose that conserved residues in domains I and II synergize to form the functional face of GDI, and that domain II mediates a critical step in Rab recycling during vesicle fusion.
==About this Structure==
==About this Structure==
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1D5T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D5T OCA].
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1D5T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5T OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Balch, W.E.]]
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[[Category: Balch, W E.]]
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[[Category: Greasley, S.E.]]
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[[Category: Greasley, S E.]]
[[Category: Heine, A.]]
[[Category: Heine, A.]]
[[Category: Kuhn, P.]]
[[Category: Kuhn, P.]]
[[Category: Moyer, B.]]
[[Category: Moyer, B.]]
[[Category: Peng, L.]]
[[Category: Peng, L.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: Zeng, K.]]
[[Category: Zeng, K.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: ultra-high resolution]]
[[Category: ultra-high resolution]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:01:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:15 2008''

Revision as of 10:13, 21 February 2008


1d5t, resolution 1.04Å

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GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR, ALPHA-ISOFORM

Overview

Guanine nucleotide dissociation inhibitor (GDI) is a 55-kDa protein that functions in vesicular membrane transport to recycle Rab GTPases. We have now determined the crystal structure of bovine alpha-GDI at ultra-high resolution (1.04 A). Refinement at this resolution highlighted a region with high mobility of its main-chain residues. This corresponded to a surface loop in the primarily alpha-helical domain II at the base of alpha-GDI containing the previously uncharacterized sequence-conserved region (SCR) 3A. Site-directed mutagenesis showed that this mobile loop plays a crucial role in binding of GDI to membranes and extraction of membrane-bound Rab. This domain, referred to as the mobile effector loop, in combination with Rab-binding residues found in the multi-sheet domain I at the apex of alpha-GDI may provide flexibility for recycling of diverse Rab GTPases. We propose that conserved residues in domains I and II synergize to form the functional face of GDI, and that domain II mediates a critical step in Rab recycling during vesicle fusion.

About this Structure

1D5T is a Single protein structure of sequence from Bos taurus with as ligand. Full crystallographic information is available from OCA.

Reference

A new functional domain of guanine nucleotide dissociation inhibitor (alpha-GDI) involved in Rab recycling., Luan P, Heine A, Zeng K, Moyer B, Greasely SE, Kuhn P, Balch WE, Wilson IA, Traffic. 2000 Mar;1(3):270-81. PMID:11208110

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