1uad: Difference between revisions
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'''Crystal structure of the RalA-GppNHp-Sec5 Ral-binding domain complex'''<br /> | '''Crystal structure of the RalA-GppNHp-Sec5 Ral-binding domain complex'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1UAD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1UAD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GNP:'>GNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: small gtp-binding protein]] | [[Category: small gtp-binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:00:33 2008'' | ||
Revision as of 18:00, 15 February 2008
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Crystal structure of the RalA-GppNHp-Sec5 Ral-binding domain complex
OverviewOverview
The sec6/8 complex or exocyst is an octameric protein complex that, functions during cell polarization by regulating the site of exocytic, vesicle docking to the plasma membrane, in concert with small GTP-binding, proteins. The Sec5 subunit of the mammalian sec6/8 complex binds Ral in a, GTP-dependent manner. Here we report the crystal structure of the complex, between the Ral-binding domain of Sec5 and RalA bound to a, non-hydrolyzable GTP analog (GppNHp) at 2.1 A resolution, providing the, first structural insights into the mechanism and specificity of sec6/8, regulation. The Sec5 Ral-binding domain folds into an immunoglobulin-like, beta-sandwich structure, which represents a novel fold for an effector of, a GTP-binding protein. The interface between the two proteins involves a, continuous antiparallel beta-sheet, similar to that found in other, effector/G-protein complexes, such as Ras and Rap1A. Specific interactions, unique to the RalA.Sec5 complex include Sec5 Thr11 and Arg27, and RalA, Glu38, which we show are required for complex formation by isothermal, titration calorimetry. Comparison of the structures of GppNHp- and, GDP-bound RalA suggests a nucleotide-dependent switch mechanism for Sec5, binding.
About this StructureAbout this Structure
1UAD is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex., Fukai S, Matern HT, Jagath JR, Scheller RH, Brunger AT, EMBO J. 2003 Jul 1;22(13):3267-78. PMID:12839989
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