1jx2
From Proteopedia
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|PDB= 1jx2 |SIZE=350|CAPTION= <scene name='initialview01'>1jx2</scene>, resolution 2.30Å | |PDB= 1jx2 |SIZE=350|CAPTION= <scene name='initialview01'>1jx2</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= dymA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 Dictyostelium discoideum]) | |GENE= dymA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 Dictyostelium discoideum]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jwy|1JWY]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jx2 OCA], [http://www.ebi.ac.uk/pdbsum/1jx2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jx2 RCSB]</span> | ||
}} | }} | ||
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[[Category: Niemann, H H.]] | [[Category: Niemann, H H.]] | ||
[[Category: Scherer, A.]] | [[Category: Scherer, A.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: GLC]] | ||
| - | [[Category: MG]] | ||
[[Category: dictyostelium]] | [[Category: dictyostelium]] | ||
[[Category: dynamin]] | [[Category: dynamin]] | ||
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[[Category: myosin]] | [[Category: myosin]] | ||
| - | ''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 21:40:16 2008'' |
Revision as of 18:40, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | dymA (Dictyostelium discoideum) | ||||||
| Related: | 1JWY
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASE DOMAIN, DETERMINED AS MYOSIN FUSION
Overview
Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In contrast to the classical switch GTPases, a force-generating function has been suggested for dynamins. Here we report the 2.3 A crystal structure of the nucleotide-free and GDP-bound GTPase domain of Dictyostelium discoideum dynamin A. The GTPase domain is the most highly conserved region among dynamins. The globular structure contains the G-protein core fold, which is extended from a six-stranded beta-sheet to an eight-stranded one by a 55 amino acid insertion. This topologically unique insertion distinguishes dynamins from other subfamilies of GTP-binding proteins. An additional N-terminal helix interacts with the C-terminal helix of the GTPase domain, forming a hydrophobic groove, which could be occupied by C-terminal parts of dynamin not present in our construct. The lack of major conformational changes between the nucleotide-free and the GDP-bound state suggests that mechanochemical rearrangements in dynamin occur during GTP binding, GTP hydrolysis or phosphate release and are not linked to loss of GDP.
About this Structure
1JX2 is a Protein complex structure of sequences from Dictyostelium discoideum. Full crystallographic information is available from OCA.
Reference
Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms., Niemann HH, Knetsch ML, Scherer A, Manstein DJ, Kull FJ, EMBO J. 2001 Nov 1;20(21):5813-21. PMID:11689422
Page seeded by OCA on Sun Mar 30 21:40:16 2008
