2fmx: Difference between revisions
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|PDB= 2fmx |SIZE=350|CAPTION= <scene name='initialview01'>2fmx</scene>, resolution 1.82Å | |PDB= 2fmx |SIZE=350|CAPTION= <scene name='initialview01'>2fmx</scene>, resolution 1.82Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2fa9|2FA9]], [[1f6b|1F6B]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmx OCA], [http://www.ebi.ac.uk/pdbsum/2fmx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fmx RCSB]</span> | |||
}} | }} | ||
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[[Category: Rao, Y.]] | [[Category: Rao, Y.]] | ||
[[Category: Yuan, C.]] | [[Category: Yuan, C.]] | ||
[[Category: cop ii assembly]] | [[Category: cop ii assembly]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
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[[Category: sar1]] | [[Category: sar1]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:05:03 2008'' | ||
Revision as of 00:05, 31 March 2008
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| 2fmx, resolution 1.82Å | |||||||||||||
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| Ligands: | GDP, MG, SO4 | ||||||||||||
| Related: | 2FA9, 1F6B
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg(2+)
Overview
Mg2+ is essential for guanosine triphosphatase activity and plays key roles in guanine nucleotide binding and preserving the structural integrity of GTP-binding proteins. To understand the structural basis for Mg2+ function during the GDP/GTP exchange process, we determined the crystal structure of Delta9-Sar1-GDP at low Mg2+ concentration at 1.8A. Two Sar1-GDP molecules in the crystal form a dimer with Mg2+ presenting only in molecule B but not in molecule A. The absence of Mg2+ induces significant conformational changes in the switch I region in molecule A that shows similarities with those of Ha-Ras bound to Sos. The current structure reveals an important regulatory role for Mg2+. We suggest that guanine nucleotide exchange factor may utilize this feature to generate an open conformation for GDP/GTP exchange. Furthermore, we propose a mechanism for COPII assembly and disassembly in which dimerization of Sar1 plays an important role.
About this Structure
2FMX is a Single protein structure of sequence from Cricetulus griseus. Full crystallographic information is available from OCA.
Reference
An open conformation of switch I revealed by Sar1-GDP crystal structure at low Mg2+., Rao Y, Bian C, Yuan C, Li Y, Chen L, Ye X, Huang Z, Huang M, Biochem Biophys Res Commun. 2006 Sep 29;348(3):908-15. Epub 2006 Aug 1. PMID:16899220
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