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1rrg

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Revision as of 23:42, 20 November 2007 by OCA (Talk | contribs)
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1rrg, resolution 2.4Å

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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 with MG and GDP as ligands. 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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