1rrg
From Proteopedia
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|PDB= 1rrg |SIZE=350|CAPTION= <scene name='initialview01'>1rrg</scene>, resolution 2.4Å | |PDB= 1rrg |SIZE=350|CAPTION= <scene name='initialview01'>1rrg</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rrg OCA], [http://www.ebi.ac.uk/pdbsum/1rrg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rrg RCSB]</span> | ||
}} | }} | ||
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[[Category: Greasley, S E.]] | [[Category: Greasley, S E.]] | ||
[[Category: Jhoti, H.]] | [[Category: Jhoti, H.]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
[[Category: gdp-binding]] | [[Category: gdp-binding]] | ||
[[Category: homodimer]] | [[Category: homodimer]] | ||
| Line 32: | Line 33: | ||
[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:32:00 2008'' |
Revision as of 20:32, 30 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, DIMERIC CRYSTAL FORM
Overview
The ARFs are a family of 21,000 M(r) proteins with biological roles in constitutive secretion and activation of phospholipase D. The structure of ARF-1 complexed to GDP determined from two crystal forms reveals a topology that is similar to that of the protein p21 ras with two differences: an additional amino-terminal helix and an extra beta-strand. The Mg2+ ion in ARF-1 displays a five-coordination sphere; this feature is not seen in p21 ras, due to a shift in the relative position of the DXXG motif between the two proteins. The occurrence of a dimer in one crystal form suggests that ARF-1 may dimerize during its biological function. The dimer interface involves a region of the ARF-1 molecule that is analogous to the effector domain in p21 ras and may mediate interactions with its effectors.
About this Structure
1RRG is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms., Greasley SE, Jhoti H, Teahan C, Solari R, Fensome A, Thomas GM, Cockcroft S, Bax B, Nat Struct Biol. 1995 Sep;2(9):797-806. PMID:7552752
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