1rrf
From Proteopedia
(New page: 200px<br /><applet load="1rrf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rrf, resolution 3.0Å" /> '''NON-MYRISTOYLATED RAT...) |
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| - | [[Image:1rrf.gif|left|200px]]<br /><applet load="1rrf" size=" | + | [[Image:1rrf.gif|left|200px]]<br /><applet load="1rrf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rrf, resolution 3.0Å" /> | caption="1rrf, resolution 3.0Å" /> | ||
'''NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, MONOMERIC CRYSTAL FORM'''<br /> | '''NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, MONOMERIC CRYSTAL FORM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ARFs are a family of 21,000 M(r) proteins with biological roles in | + | 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== | ==About this Structure== | ||
| - | 1RRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RRF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bax, B.]] | [[Category: Bax, B.]] | ||
| - | [[Category: Greasley, S | + | [[Category: Greasley, S E.]] |
[[Category: Jhoti, H.]] | [[Category: Jhoti, H.]] | ||
[[Category: GDP]] | [[Category: GDP]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:47 2008'' |
Revision as of 12:53, 21 February 2008
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NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, MONOMERIC 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
1RRF is a Single protein structure of sequence from Rattus norvegicus with and 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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