1hur
From Proteopedia
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|PDB= 1hur |SIZE=350|CAPTION= <scene name='initialview01'>1hur</scene>, resolution 2.0Å | |PDB= 1hur |SIZE=350|CAPTION= <scene name='initialview01'>1hur</scene>, resolution 2.0Å | ||
|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= HARF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= HARF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hur OCA], [http://www.ebi.ac.uk/pdbsum/1hur PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hur RCSB]</span> | ||
}} | }} | ||
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[[Category: Kahn, R A.]] | [[Category: Kahn, R A.]] | ||
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
[[Category: gdp-binding]] | [[Category: gdp-binding]] | ||
[[Category: membrane traffickin]] | [[Category: membrane traffickin]] | ||
[[Category: non-myristoylated]] | [[Category: non-myristoylated]] | ||
| - | ''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 21:10:40 2008'' |
Revision as of 18:10, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | HARF1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED
Overview
ADP-ribosylation factors (ARFs) are essential and ubiquitous in eukaryotes, being involved in vesicular transport and functioning as an activator of phospholipase D (refs 1, 2) and cholera toxin. The functions of ARF proteins in membrane traffic and organelle integrity are intimately tied to its reversible association with membranes and specific interactions with membrane phospholipids. One common feature of these functions is their regulation by the binding and hydrolysis of GTP. Here we report the three-dimensional structure of full-length human ARF1 (M(r) 21,000) in its GDP-bound non-myristoylated form. The presence of a unique amino-terminal alpha-helix and loop, together with differences in Mg2+ ligation and the existence of a non-crystallographic dimer, set this structure apart from other GTP-binding proteins. These features provide a structural basis for the GTP-dependent modulation of membrane affinity, the lack of intrinsic GTPase activity, and the nature of effector binding surfaces.
About this Structure
1HUR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the human ADP-ribosylation factor 1 complexed with GDP., Amor JC, Harrison DH, Kahn RA, Ringe D, Nature. 1994 Dec 15;372(6507):704-8. PMID:7990966
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