1jx2

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[[Image:1jx2.gif|left|200px]]
[[Image:1jx2.gif|left|200px]]
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{{Structure
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|PDB= 1jx2 |SIZE=350|CAPTION= <scene name='initialview01'>1jx2</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1jx2", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= dymA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 Dictyostelium discoideum])
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|DOMAIN=
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{{STRUCTURE_1jx2| PDB=1jx2 | SCENE= }}
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|RELATEDENTRY=[[1jwy|1JWY]]
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|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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}}
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'''CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASE DOMAIN, DETERMINED AS MYOSIN FUSION'''
'''CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASE DOMAIN, DETERMINED AS MYOSIN FUSION'''
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[[Category: Niemann, H H.]]
[[Category: Niemann, H H.]]
[[Category: Scherer, A.]]
[[Category: Scherer, A.]]
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[[Category: dictyostelium]]
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[[Category: Dictyostelium]]
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[[Category: dynamin]]
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[[Category: Dynamin]]
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[[Category: fusion-protein]]
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[[Category: Fusion-protein]]
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[[Category: gtpase]]
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[[Category: Gtpase]]
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[[Category: myosin]]
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[[Category: Myosin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:01:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:40:16 2008''
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Revision as of 19:01, 2 May 2008

Template:STRUCTURE 1jx2

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 Fri May 2 22:01:56 2008

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