1moz
From Proteopedia
(New page: 200px<br /><applet load="1moz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1moz, resolution 3.17Å" /> '''ADP-ribosylation fac...) |
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| - | [[Image:1moz.gif|left|200px]]<br /><applet load="1moz" size=" | + | [[Image:1moz.gif|left|200px]]<br /><applet load="1moz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1moz, resolution 3.17Å" /> | caption="1moz, resolution 3.17Å" /> | ||
'''ADP-ribosylation factor-like 1 (ARL1) from Saccharomyces cerevisiae'''<br /> | '''ADP-ribosylation factor-like 1 (ARL1) from Saccharomyces cerevisiae'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Structures were determined by x-ray crystallography for two members of the | + | Structures were determined by x-ray crystallography for two members of the ADP-ribosylation factor (ARF) family of regulatory GTPases, yeast ARF1 and ARL1, and were compared with previously determined structures of human ARF1 and ARF6. These analyses revealed an overall conserved fold but differences in primary sequence and length, particularly in an N-terminal loop, lead to differences in nucleotide and divalent metal binding. Packing of hydrophobic residues is central to the interplay between the N-terminal alpha-helix, switch I, and the interswitch region, which along with differences in surface electrostatics provide explanations for the different biophysical and biochemical properties of ARF and ARF-like proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1MOZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with GDP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MOZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Amor, J | + | [[Category: Amor, J C.]] |
[[Category: Cheng, X.]] | [[Category: Cheng, X.]] | ||
| - | [[Category: Horton, J | + | [[Category: Horton, J R.]] |
| - | [[Category: Kahn, R | + | [[Category: Kahn, R A.]] |
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: Sullards, C.]] | [[Category: Sullards, C.]] | ||
| Line 24: | Line 24: | ||
[[Category: gtp-binding]] | [[Category: gtp-binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:31 2008'' |
Revision as of 11:57, 21 February 2008
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ADP-ribosylation factor-like 1 (ARL1) from Saccharomyces cerevisiae
Overview
Structures were determined by x-ray crystallography for two members of the ADP-ribosylation factor (ARF) family of regulatory GTPases, yeast ARF1 and ARL1, and were compared with previously determined structures of human ARF1 and ARF6. These analyses revealed an overall conserved fold but differences in primary sequence and length, particularly in an N-terminal loop, lead to differences in nucleotide and divalent metal binding. Packing of hydrophobic residues is central to the interplay between the N-terminal alpha-helix, switch I, and the interswitch region, which along with differences in surface electrostatics provide explanations for the different biophysical and biochemical properties of ARF and ARF-like proteins.
About this Structure
1MOZ is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.
Reference
Structures of yeast ARF2 and ARL1: distinct roles for the N terminus in the structure and function of ARF family GTPases., Amor JC, Horton JR, Zhu X, Wang Y, Sullards C, Ringe D, Cheng X, Kahn RA, J Biol Chem. 2001 Nov 9;276(45):42477-84. Epub 2001 Sep 4. PMID:11535602
Page seeded by OCA on Thu Feb 21 13:57:31 2008
Categories: Saccharomyces cerevisiae | Single protein | Amor, J C. | Cheng, X. | Horton, J R. | Kahn, R A. | Ringe, D. | Sullards, C. | Wang, Y. | Zhu, X. | GDP | Gtp-binding
