1nm1

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{{STRUCTURE_1nm1| PDB=1nm1 | SCENE= }}
 
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===Crystal Structure of D. Dicsoideum Actin Complexed With Gelsolin Segment 1 and Mg ATP at 1.8 A Resolution===
 
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{{ABSTRACT_PUBMED_12732734}}
 
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==Disease==
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==Crystal Structure of D. Dicsoideum Actin Complexed With Gelsolin Segment 1 and Mg ATP at 1.8 A Resolution==
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[[http://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:[http://omim.org/entry/105120 105120]]; also known as familial amyloidosis Finnish type. AMYL5 is a hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure.<ref>PMID:2157434</ref><ref>PMID:2153578</ref><ref>PMID:2176481</ref><ref>PMID:1338910</ref>
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<StructureSection load='1nm1' size='340' side='right'caption='[[1nm1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1nm1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dga 1dga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NM1 FirstGlance]. <br>
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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]] 1.8&#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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO2:SULFUR+DIOXIDE'>SO2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nm1 OCA], [https://pdbe.org/1nm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nm1 RCSB], [https://www.ebi.ac.uk/pdbsum/1nm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nm1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACT1_DICDI ACT1_DICDI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/1nm1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nm1 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structures of Saccharomyces cerevisiae, Dictyostelium, and Caenorhabditis elegans actin bound to gelsolin segment-1 have been solved and refined at resolutions between 1.9 and 1.75 A. These structures reveal several features relevant to the ATP hydrolytic mechanism, including identification of the nucleophilic water and the roles of Gln-137 and His-161 in positioning and activating the catalytic water, respectively. The involvement of these residues in the catalytic mechanism is consistent with yeast genetics studies. This work highlights both structural and mechanistic similarities with the small and trimeric G proteins and restricts the types of mechanisms responsible for the considerable enhancement of ATP hydrolysis associated with actin polymerization. The conservation of functionalities involved in nucleotide binding and catalysis also provide insights into the mechanistic features of members of the family of actin-related proteins.
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==Function==
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The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism.,Vorobiev S, Strokopytov B, Drubin DG, Frieden C, Ono S, Condeelis J, Rubenstein PA, Almo SC Proc Natl Acad Sci U S A. 2003 May 13;100(10):5760-5. Epub 2003 May 5. PMID:12732734<ref>PMID:12732734</ref>
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[[http://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.<ref>PMID:20393563</ref>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[1nm1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dga 1dga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NM1 OCA].
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</div>
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<div class="pdbe-citations 1nm1" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Actin|Actin]]
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*[[Actin 3D structures|Actin 3D structures]]
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*[[Gelsolin|Gelsolin]]
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*[[Gelsolin 3D structures|Gelsolin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:012732734</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Dictyostelium discoideum]]
[[Category: Dictyostelium discoideum]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Almo, S C.]]
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[[Category: Large Structures]]
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[[Category: Condeelis, J.]]
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[[Category: Almo SC]]
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[[Category: Vorobiev, S M.]]
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[[Category: Condeelis J]]
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[[Category: Welti, S.]]
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[[Category: Vorobiev SM]]
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[[Category: Actin]]
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[[Category: Welti S]]
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[[Category: Actin-associated protein]]
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[[Category: Cytoskeleton organization]]
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[[Category: Gelsolin]]
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[[Category: Structural protein]]
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Current revision

Crystal Structure of D. Dicsoideum Actin Complexed With Gelsolin Segment 1 and Mg ATP at 1.8 A Resolution

PDB ID 1nm1

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