1bof
From Proteopedia
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|PDB= 1bof |SIZE=350|CAPTION= <scene name='initialview01'>1bof</scene>, resolution 2.2Å | |PDB= 1bof |SIZE=350|CAPTION= <scene name='initialview01'>1bof</scene>, resolution 2.2Å | ||
|SITE= <scene name='pdbsite=MG:Octahedral+Mg+Binding+Site'>MG</scene> | |SITE= <scene name='pdbsite=MG:Octahedral+Mg+Binding+Site'>MG</scene> | ||
| - | |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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bof OCA], [http://www.ebi.ac.uk/pdbsum/1bof PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bof RCSB]</span> | ||
}} | }} | ||
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[[Category: Coleman, D E.]] | [[Category: Coleman, D E.]] | ||
[[Category: Sprang, S R.]] | [[Category: Sprang, S R.]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: SO4]] | ||
[[Category: g protein]] | [[Category: g protein]] | ||
[[Category: gtp-ase]] | [[Category: gtp-ase]] | ||
[[Category: signal transduction protein]] | [[Category: signal transduction protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:05:03 2008'' |
Revision as of 16:05, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GI-ALPHA-1 BOUND TO GDP AND MAGNESIUM
Overview
The effect of Mg2+ binding on the conformation of the inactive GDP-bound complex of the heterotrimeric G protein alpha subunit Gi alpha 1 has been investigated by X-ray crystallography. Crystal structures of the Gi alpha 1.GDP complex were determined after titration with 5, 10, 100, and 200 mM Mg2+. Comparison of these structures with that of the Mg2+-free complex revealed Mg2+ bound at the same site as observed in the structure of the active, Gi alpha 1. GTP gamma S.Mg2+-bound complex of Gi alpha 1, with a similar coordination scheme except for the substitution of a water molecule for an oxygen ligand of the gamma-phosphate of Gi alpha 1.GTP gamma S. Mg2+. In contrast to the GDP.Mg2+ complex of Gt alpha and of other G proteins, switch I residues of Gi alpha 1 participate in Mg2+ binding and undergo conformational changes as a consequence of Mg2+ binding. Partial order is induced in switch II, which is disordered in the Mg2+-free complex, but no order is observed in the switch III region. This contrasts with the GDP.Mg2+ complex of Gt alpha in which both switch II and III switch are ordered. Mg2+ binding also induces binding of an SO42- molecule to the active site in a manner which may mimic a Gi alpha 1.GDP.PO42-.Mg2+ product complex. Implications of these findings are discussed.
About this Structure
1BOF is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structures of the G protein Gi alpha 1 complexed with GDP and Mg2+: a crystallographic titration experiment., Coleman DE, Sprang SR, Biochemistry. 1998 Oct 13;37(41):14376-85. PMID:9772163
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