4h1v

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4h1v]] 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=4H1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H1V FirstGlance]. <br>
<table><tr><td colspan='2'>[[4h1v]] 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=4H1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H1V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene></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=4h1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h1v OCA], [https://pdbe.org/4h1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h1v RCSB], [https://www.ebi.ac.uk/pdbsum/4h1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h1v ProSAT]</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=4h1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h1v OCA], [https://pdbe.org/4h1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h1v RCSB], [https://www.ebi.ac.uk/pdbsum/4h1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h1v ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/DNM1L_HUMAN DNM1L_HUMAN] Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into ring-like structures which wrap around the scission site to constict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. Required for normal brain development. Facilitates developmentally-regulated apoptosis during neural tube development. Required for a normal rate of cytochrome c release and caspase activation during apoptosis. Also required for mitochondrial fission during mitosis. Required for programmed necrosis execution. May be involved in vesicle transport.<ref>PMID:9570752</ref> <ref>PMID:9786947</ref> <ref>PMID:11514614</ref> <ref>PMID:12499366</ref> <ref>PMID:12618434</ref> <ref>PMID:15208300</ref> <ref>PMID:17015472</ref> <ref>PMID:17301055</ref> <ref>PMID:17553808</ref> <ref>PMID:17460227</ref> <ref>PMID:18695047</ref> <ref>PMID:18838687</ref> <ref>PMID:19638400</ref> <ref>PMID:19411255</ref> <ref>PMID:19342591</ref> <ref>PMID:20688057</ref> Isoform 1 and isoform 4 inhibit peroxisomal division when overexpressed.<ref>PMID:9570752</ref> <ref>PMID:9786947</ref> <ref>PMID:11514614</ref> <ref>PMID:12499366</ref> <ref>PMID:12618434</ref> <ref>PMID:15208300</ref> <ref>PMID:17015472</ref> <ref>PMID:17301055</ref> <ref>PMID:17553808</ref> <ref>PMID:17460227</ref> <ref>PMID:18695047</ref> <ref>PMID:18838687</ref> <ref>PMID:19638400</ref> <ref>PMID:19411255</ref> <ref>PMID:19342591</ref> <ref>PMID:20688057</ref>
[https://www.uniprot.org/uniprot/DNM1L_HUMAN DNM1L_HUMAN] Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into ring-like structures which wrap around the scission site to constict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. Required for normal brain development. Facilitates developmentally-regulated apoptosis during neural tube development. Required for a normal rate of cytochrome c release and caspase activation during apoptosis. Also required for mitochondrial fission during mitosis. Required for programmed necrosis execution. May be involved in vesicle transport.<ref>PMID:9570752</ref> <ref>PMID:9786947</ref> <ref>PMID:11514614</ref> <ref>PMID:12499366</ref> <ref>PMID:12618434</ref> <ref>PMID:15208300</ref> <ref>PMID:17015472</ref> <ref>PMID:17301055</ref> <ref>PMID:17553808</ref> <ref>PMID:17460227</ref> <ref>PMID:18695047</ref> <ref>PMID:18838687</ref> <ref>PMID:19638400</ref> <ref>PMID:19411255</ref> <ref>PMID:19342591</ref> <ref>PMID:20688057</ref> Isoform 1 and isoform 4 inhibit peroxisomal division when overexpressed.<ref>PMID:9570752</ref> <ref>PMID:9786947</ref> <ref>PMID:11514614</ref> <ref>PMID:12499366</ref> <ref>PMID:12618434</ref> <ref>PMID:15208300</ref> <ref>PMID:17015472</ref> <ref>PMID:17301055</ref> <ref>PMID:17553808</ref> <ref>PMID:17460227</ref> <ref>PMID:18695047</ref> <ref>PMID:18838687</ref> <ref>PMID:19638400</ref> <ref>PMID:19411255</ref> <ref>PMID:19342591</ref> <ref>PMID:20688057</ref>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Human dynamin-1-like protein (DNM1L) is a GTP-driven molecular machine that segregates mitochondria and peroxisomes. To obtain insights into its catalytic mechanism, we determined crystal structures of a construct comprising the GTPase domain and the bundle signaling element (BSE) in the nucleotide-free and GTP-analogue-bound states. The GTPase domain of DNM1L is structurally related to that of dynamin and binds the nucleotide 5'-Guanylyl-imidodiphosphate (GMP-PNP) via five highly conserved motifs, whereas the BSE folds into a pocket at the opposite side. Based on these structures, the GTPase center was systematically mapped by alanine mutagenesis and kinetic measurements. Thus, residues essential for the GTPase reaction were characterized, among them Lys38, Ser39 and Ser40 in the phosphate binding loop, Thr59 from switch I, Asp146 and Gly149 from switch II, Lys216 and Asp218 in the G4 element, as well as Asn246 in the G5 element. Also, mutated Glu81 and Glu82 in the unique 16-residue insertion of DNM1L influence the activity significantly. Mutations of Gln34, Ser35, and Asp190 in the predicted assembly interface interfered with dimerization of the GTPase domain induced by a transition state analogue and led to a loss of the lipid-stimulated GTPase activity. Our data point to related catalytic mechanisms of DNM1L and dynamin involving dimerization of their GTPase domains.
 
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Functional Mapping of Human Dynamin-1-Like GTPase Domain Based on X-ray Structure Analyses.,Wenger J, Klinglmayr E, Frohlich C, Eibl C, Gimeno A, Hessenberger M, Puehringer S, Daumke O, Goettig P PLoS One. 2013 Aug 19;8(8):e71835. doi: 10.1371/journal.pone.0071835. PMID:23977156<ref>PMID:23977156</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 4h1v" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>

Current revision

GMP-PNP bound dynamin-1-like protein GTPase-GED fusion

PDB ID 4h1v

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