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3cjc

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[[Image:3cjc.jpg|left|200px]]
 
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{{Structure
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==Actin dimer cross-linked by V. cholerae MARTX toxin and complexed with DNase I and Gelsolin-segment 1==
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|PDB= 3cjc |SIZE=350|CAPTION= <scene name='initialview01'>3cjc</scene>, resolution 3.900&Aring;
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<StructureSection load='3cjc' size='340' side='right'caption='[[3cjc]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+D+270'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+D+271'>AC2</scene>, <scene name='pdbsite=AC3:Ca+Binding+Site+For+Residue+A+401'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+D+272'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+D+273'>AC5</scene>, <scene name='pdbsite=AC6:So4+Binding+Site+For+Residue+D+274'>AC6</scene>, <scene name='pdbsite=AC7:So4+Binding+Site+For+Residue+G+126'>AC7</scene>, <scene name='pdbsite=AC8:So4+Binding+Site+For+Residue+A+402'>AC8</scene>, <scene name='pdbsite=AC9:So4+Binding+Site+For+Residue+D+275'>AC9</scene>, <scene name='pdbsite=BC1:Ca+Binding+Site+For+Residue+G+127'>BC1</scene> and <scene name='pdbsite=BC2:Atp+Binding+Site+For+Residue+A+403'>BC2</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[3cjc]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CJC FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribonuclease_I Deoxyribonuclease I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.1 3.1.21.1] </span>
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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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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|GENE= GSN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3cjb|3cjb]]</div></td></tr>
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00022 Actin], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00012 ACTIN], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00262 GEL], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00476 DNaseIc]</span>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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|RELATEDENTRY=[[3cjb|3CJB]]
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Deoxyribonuclease_I Deoxyribonuclease I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.1 3.1.21.1] </span></td></tr>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cjc OCA], [http://www.ebi.ac.uk/pdbsum/3cjc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3cjc RCSB]</span>
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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=3cjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cjc OCA], [https://pdbe.org/3cjc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cjc RCSB], [https://www.ebi.ac.uk/pdbsum/3cjc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cjc ProSAT]</span></td></tr>
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}}
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</table>
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== Disease ==
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[[https://www.uniprot.org/uniprot/GELS_HUMAN GELS_HUMAN]] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:[https://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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== Function ==
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[[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [[https://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> [[https://www.uniprot.org/uniprot/DNAS1_BOVIN DNAS1_BOVIN]] Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (By similarity).
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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/cj/3cjc_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=3cjc 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 Gram-negative bacterium Vibrio cholerae is the causative agent of a severe diarrheal disease that afflicts three to five million persons annually, causing up to 200,000 deaths. Nearly all V. cholerae strains produce a large multifunctional-autoprocessing RTX toxin (MARTX(Vc)), which contributes significantly to the pathogenesis of cholera in model systems. The actin cross-linking domain (ACD) of MARTX(Vc) directly catalyzes a covalent cross-linking of monomeric G-actin into oligomeric chains and causes cell rounding, but the nature of the cross-linked bond and the mechanism of the actin cytoskeleton disruption remained elusive. To elucidate the mechanism of ACD action and effect on actin, we identified the covalent cross-link bond between actin protomers using limited proteolysis, X-ray crystallography, and mass spectrometry. We report here that ACD catalyzes the formation of an intermolecular iso-peptide bond between residues E270 and K50 located in the hydrophobic and the DNaseI-binding loops of actin, respectively. Mutagenesis studies confirm that no other residues on actin can be cross-linked by ACD both in vitro and in vivo. This cross-linking locks actin protomers into an orientation different from that of F-actin, resulting in strong inhibition of actin polymerization. This report describes a microbial toxin mechanism acting via iso-peptide bond cross-linking between host proteins and is, to the best of our knowledge, the only known example of a peptide linkage between nonterminal glutamate and lysine side chains.
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'''Actin dimer cross-linked by V. cholerae MARTX toxin and complexed with DNase I and Gelsolin-segment 1'''
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Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin.,Kudryashov DS, Durer ZA, Ytterberg AJ, Sawaya MR, Pashkov I, Prochazkova K, Yeates TO, Loo RR, Loo JA, Satchell KJ, Reisler E Proc Natl Acad Sci U S A. 2008 Nov 25;105(47):18537-42. Epub 2008 Nov 17. PMID:19015515<ref>PMID:19015515</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 3cjc" style="background-color:#fffaf0;"></div>
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==Disease==
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==See Also==
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Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=137350 137350]]
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*[[Actin 3D structures|Actin 3D structures]]
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*[[Gelsolin 3D structures|Gelsolin 3D structures]]
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==About this Structure==
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== References ==
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3CJC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CJC OCA].
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Deoxyribonuclease I]]
[[Category: Deoxyribonuclease I]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Protein complex]]
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[[Category: Kudryashov, D S]]
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[[Category: Kudryashov, D S.]]
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[[Category: Pashkov, I]]
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[[Category: Pashkov, I.]]
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[[Category: Reisler, E]]
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[[Category: Reisler, E.]]
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[[Category: Sawaya, M R]]
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[[Category: Sawaya, M R.]]
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[[Category: Yeates, T O]]
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[[Category: Yeates, T O.]]
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[[Category: Actin capping]]
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[[Category: acetylation]]
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[[Category: Actin-binding]]
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[[Category: actin capping]]
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[[Category: Alternative initiation]]
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[[Category: actin-binding]]
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[[Category: Amyloid]]
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[[Category: alternative initiation]]
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[[Category: Apoptosis]]
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[[Category: amyloid]]
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[[Category: Atp-binding]]
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[[Category: apoptosis]]
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[[Category: Cross-linked dimer]]
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[[Category: atp-binding]]
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[[Category: Cytoskeleton]]
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[[Category: calcium]]
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[[Category: Disease mutation]]
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[[Category: cross-linked dimer]]
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[[Category: Endonuclease]]
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[[Category: cytoplasm]]
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[[Category: Glycoprotein]]
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[[Category: cytoskeleton]]
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[[Category: Hydrolase]]
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[[Category: disease mutation]]
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[[Category: Methylation]]
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[[Category: endonuclease]]
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[[Category: Muscle protein]]
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[[Category: glycoprotein]]
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[[Category: Nuclease]]
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[[Category: hydrolase]]
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[[Category: Nucleotide-binding]]
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[[Category: methylation]]
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[[Category: Nucleus]]
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[[Category: muscle protein]]
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[[Category: Phosphoprotein]]
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[[Category: nuclease]]
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[[Category: Secreted]]
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[[Category: nucleotide-binding]]
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[[Category: Structural protein]]
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[[Category: nucleus]]
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[[Category: Structural protein-hydrolase complex]]
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[[Category: phosphoprotein]]
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[[Category: polymorphism]]
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[[Category: secreted]]
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[[Category: structural protein]]
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[[Category: structural protein/hydrolase complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:32:31 2008''
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Current revision

Actin dimer cross-linked by V. cholerae MARTX toxin and complexed with DNase I and Gelsolin-segment 1

PDB ID 3cjc

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