1gnd: Difference between revisions
New page: left|200px<br /><applet load="1gnd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gnd, resolution 1.81Å" /> '''GUANINE NUCLEOTIDE D... |
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[[Image:1gnd.gif|left|200px]]<br /><applet load="1gnd" size=" | [[Image:1gnd.gif|left|200px]]<br /><applet load="1gnd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1gnd, resolution 1.81Å" /> | caption="1gnd, resolution 1.81Å" /> | ||
'''GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR, ALPHA-ISOFORM'''<br /> | '''GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR, ALPHA-ISOFORM'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the bovine alpha-isoform of Rab GDP-dissociation | The crystal structure of the bovine alpha-isoform of Rab GDP-dissociation inhibitor (GDI), which functions in vesicle-membrane transport to recycle and regulate Rab GTPases, has been determined to a resolution of 1.81 A. GDI is constructed of two main structural units, a large complex multisheet domain I and a smaller alpha-helical domain II. The structural organization of domain I is surprisingly closely related to FAD-containing monooxygenases and oxidases. Sequence-conserved regions common to GDI and the choroideraemia gene product, which delivers Rab to catalytic subunits of Rab geranylgeranyltransferase II, are clustered on one face of the molecule. The two most sequence-conserved regions, which form a compact structure at the apex of GDI, are shown by site-directed mutagenesis to play a critical role in the binding of Rab proteins. | ||
==About this Structure== | ==About this Structure== | ||
1GND is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | 1GND is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GND OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Balch, W | [[Category: Balch, W E.]] | ||
[[Category: Huang, M.]] | [[Category: Huang, M.]] | ||
[[Category: Metteson, J.]] | [[Category: Metteson, J.]] | ||
[[Category: Schalk, I.]] | [[Category: Schalk, I.]] | ||
[[Category: Stura, E | [[Category: Stura, E A.]] | ||
[[Category: Tandon, A.]] | [[Category: Tandon, A.]] | ||
[[Category: Wilson, I | [[Category: Wilson, I A.]] | ||
[[Category: Wu, S | [[Category: Wu, S K.]] | ||
[[Category: Zeng, K.]] | [[Category: Zeng, K.]] | ||
[[Category: gtpase activation]] | [[Category: gtpase activation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:54 2008'' | ||
Revision as of 13:51, 21 February 2008
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GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR, ALPHA-ISOFORM
OverviewOverview
The crystal structure of the bovine alpha-isoform of Rab GDP-dissociation inhibitor (GDI), which functions in vesicle-membrane transport to recycle and regulate Rab GTPases, has been determined to a resolution of 1.81 A. GDI is constructed of two main structural units, a large complex multisheet domain I and a smaller alpha-helical domain II. The structural organization of domain I is surprisingly closely related to FAD-containing monooxygenases and oxidases. Sequence-conserved regions common to GDI and the choroideraemia gene product, which delivers Rab to catalytic subunits of Rab geranylgeranyltransferase II, are clustered on one face of the molecule. The two most sequence-conserved regions, which form a compact structure at the apex of GDI, are shown by site-directed mutagenesis to play a critical role in the binding of Rab proteins.
About this StructureAbout this Structure
1GND is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Structure and mutational analysis of Rab GDP-dissociation inhibitor., Schalk I, Zeng K, Wu SK, Stura EA, Matteson J, Huang M, Tandon A, Wilson IA, Balch WE, Nature. 1996 May 2;381(6577):42-8. PMID:8609986
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