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==Crystal structure of nucleotide-free human dynamin1==
==Crystal structure of nucleotide-free human dynamin1==
<StructureSection load='3snh' size='340' side='right' caption='[[3snh]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
<StructureSection load='3snh' size='340' side='right'caption='[[3snh]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3snh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SNH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SNH FirstGlance]. <br>
<table><tr><td colspan='2'>[[3snh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SNH FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNM, DNM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dynamin_GTPase Dynamin GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.5 3.6.5.5] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3snh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3snh OCA], [https://pdbe.org/3snh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3snh RCSB], [https://www.ebi.ac.uk/pdbsum/3snh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3snh ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3snh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3snh OCA], [http://pdbe.org/3snh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3snh RCSB], [http://www.ebi.ac.uk/pdbsum/3snh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3snh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DYN1_HUMAN DYN1_HUMAN]] Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.  
[https://www.uniprot.org/uniprot/DYN1_HUMAN DYN1_HUMAN] Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dynamin is a mechanochemical GTPase that oligomerizes around the neck of clathrin-coated pits and catalyses vesicle scission in a GTP-hydrolysis-dependent manner. The molecular details of oligomerization and the mechanism of the mechanochemical coupling are currently unknown. Here we present the crystal structure of human dynamin 1 in the nucleotide-free state with a four-domain architecture comprising the GTPase domain, the bundle signalling element, the stalk and the pleckstrin homology domain. Dynamin 1 oligomerized in the crystals via the stalks, which assemble in a criss-cross fashion. The stalks further interact via conserved surfaces with the pleckstrin homology domain and the bundle signalling element of the neighbouring dynamin molecule. This intricate domain interaction rationalizes a number of disease-related mutations in dynamin 2 and suggests a structural model for the mechanochemical coupling that reconciles previous models of dynamin function.
 
Crystal structure of nucleotide-free dynamin.,Faelber K, Posor Y, Gao S, Held M, Roske Y, Schulze D, Haucke V, Noe F, Daumke O Nature. 2011 Sep 18;477(7366):556-60. doi: 10.1038/nature10369. PMID:21927000<ref>PMID:21927000</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3snh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dynamin GTPase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Daumke, O]]
[[Category: Daumke O]]
[[Category: Faelber, K]]
[[Category: Faelber K]]
[[Category: Endocytosis]]
[[Category: Hydrolase]]

Latest revision as of 16:02, 14 March 2024

Crystal structure of nucleotide-free human dynamin1Crystal structure of nucleotide-free human dynamin1

Structural highlights

3snh is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DYN1_HUMAN Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.

3snh, resolution 3.70Å

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