1jx2
From Proteopedia
(New page: 200px<br /><applet load="1jx2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jx2, resolution 2.30Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1jx2.gif|left|200px]]<br /><applet load="1jx2" size=" | + | [[Image:1jx2.gif|left|200px]]<br /><applet load="1jx2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jx2, resolution 2.30Å" /> | caption="1jx2, resolution 2.30Å" /> | ||
'''CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASE DOMAIN, DETERMINED AS MYOSIN FUSION'''<br /> | '''CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASE DOMAIN, DETERMINED AS MYOSIN FUSION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In | + | 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== | ==About this Structure== | ||
| - | 1JX2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with GLC, MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1JX2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JX2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dictyostelium discoideum]] | [[Category: Dictyostelium discoideum]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Knetsch, M | + | [[Category: Knetsch, M L.W.]] |
| - | [[Category: Kull, F | + | [[Category: Kull, F J.]] |
| - | [[Category: Manstein, D | + | [[Category: Manstein, D J.]] |
| - | [[Category: Niemann, H | + | [[Category: Niemann, H H.]] |
[[Category: Scherer, A.]] | [[Category: Scherer, A.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: myosin]] | [[Category: myosin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:42 2008'' |
Revision as of 11:27, 21 February 2008
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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 with , and as ligands. 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 Thu Feb 21 13:27:42 2008
Categories: Dictyostelium discoideum | Protein complex | Knetsch, M L.W. | Kull, F J. | Manstein, D J. | Niemann, H H. | Scherer, A. | ADP | GLC | MG | Dictyostelium | Dynamin | Fusion-protein | Gtpase | Myosin
