5d3q

From Proteopedia

(Difference between revisions)

Revision as of 10:20, 21 June 2023

Dynamin 1 GTPase-BSE fusion dimer complexed with GDP

Structural highlights

5d3q is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
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.

Publication Abstract from PubMed

Dynamin is the prototype of a family of large multi-domain GTPases. The 100 kDa protein is a key player in clathrin-mediated endocytosis, where it cleaves off vesicles from membranes using the energy from GTP hydrolysis. We have solved the high resolution crystal structure of a fusion protein of the GTPase domain and the bundle signalling element (BSE) of dynamin 1 liganded with GDP. The structure provides a hitherto missing snapshot of the GDP state of the hydrolytic cycle of dynamin and reveals how the switch I region moves away from the active site after GTP hydrolysis and release of inorganic phosphate. Comparing our structure of the GDP state with the known structures of the GTP state, the transition state and the nucleotide-free state of dynamin 1 we describe the structural changes through the hydrolytic cycle.

Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state.,Anand R, Eschenburg S, Reubold TF Biochem Biophys Res Commun. 2016 Jan 1;469(1):76-80. doi:, 10.1016/j.bbrc.2015.11.074. Epub 2015 Nov 21. PMID:26612256^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Anand R, Eschenburg S, Reubold TF. Crystal structure of the GTPase domain and the bundle signalling element of dynamin in the GDP state. Biochem Biophys Res Commun. 2016 Jan 1;469(1):76-80. doi:, 10.1016/j.bbrc.2015.11.074. Epub 2015 Nov 21. PMID:26612256 doi:http://dx.doi.org/10.1016/j.bbrc.2015.11.074

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5d3q"

Categories: Homo sapiens | Large Structures | Anand R | Eschenburg S | Reubold TF

@@ Line 3: / Line 3: @@
 <StructureSection load='5d3q' size='340' side='right'caption='[[5d3q]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5d3q]] is a 2 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=5D3Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D3Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5d3q]] is a 2 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=5D3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D3Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNM1, DNM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5d3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d3q OCA], [https://pdbe.org/5d3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d3q RCSB], [https://www.ebi.ac.uk/pdbsum/5d3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d3q 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=5d3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d3q OCA], [http://pdbe.org/5d3q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d3q RCSB], [http://www.ebi.ac.uk/pdbsum/5d3q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d3q ProSAT]</span></td></tr>
 </table>
 == 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 ==
@@ Line 22: / Line 21: @@
 ==See Also==
 *[[Dynamin|Dynamin]]
-*[[Dynamin 3D structures|Dynamin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Anand, R]]
+[[Category: Anand R]]
-[[Category: Eschenburg, S]]
+[[Category: Eschenburg S]]
-[[Category: Reubold, T F]]
+[[Category: Reubold TF]]
-[[Category: Endocytosis]]
-[[Category: Fusion protein]]
-[[Category: Gtpase]]
-[[Category: Hydrolase]]

5d3q

From Proteopedia

Revision as of 10:20, 21 June 2023

Dynamin 1 GTPase-BSE fusion dimer complexed with GDP

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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