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1jx2

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|PDB= 1jx2 |SIZE=350|CAPTION= <scene name='initialview01'>1jx2</scene>, resolution 2.30&Aring;
|PDB= 1jx2 |SIZE=350|CAPTION= <scene name='initialview01'>1jx2</scene>, resolution 2.30&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
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|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</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])
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[[Category: myosin]]
[[Category: myosin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:09:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:24:34 2008''

Revision as of 10:24, 23 March 2008

Image:1jx2.gif


PDB ID 1jx2

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: , and
Gene: dymA (Dictyostelium discoideum)
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

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