Proteopedia

5ya6: Difference between revisions

← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='5ya6' size='340' side='right'caption='[[5ya6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='5ya6' size='340' side='right'caption='[[5ya6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ya6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YA6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ya6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YA6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 1.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5z1l|5z1l]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flaB1, MJ0891 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</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=5ya6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ya6 OCA], [https://pdbe.org/5ya6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ya6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ya6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ya6 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=5ya6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ya6 OCA], [https://pdbe.org/5ya6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ya6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ya6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ya6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FLAB1_METJA FLAB1_METJA]] Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.  
[https://www.uniprot.org/uniprot/FLAB1_METJA FLAB1_METJA] Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many archaea swim by means of archaella. While the archaellum is similar in function to its bacterial counterpart, its structure, composition, and evolution are fundamentally different. Archaella are related to archaeal and bacterial type IV pili. Despite recent advances, our understanding of molecular processes governing archaellum assembly and stability is still incomplete. Here, we determine the structures of Methanococcus archaella by X-ray crystallography and cryo-EM The crystal structure of Methanocaldococcus jannaschii FlaB1 is the first and only crystal structure of any archaellin to date at a resolution of 1.5 A, which is put into biological context by a cryo-EM reconstruction from Methanococcus maripaludis archaella at 4 A resolution created with helical single-particle analysis. Our results indicate that the archaellum is predominantly composed of FlaB1. We identify N-linked glycosylation by cryo-EM and mass spectrometry. The crystal structure reveals a highly conserved metal-binding site, which is validated by mass spectrometry and electron energy-loss spectroscopy. We show in vitro that the metal-binding site, which appears to be a widespread property of archaellin, is required for filament integrity.
 
High-resolution archaellum structure reveals a conserved metal-binding site.,Meshcheryakov VA, Shibata S, Schreiber MT, Villar-Briones A, Jarrell KF, Aizawa SI, Wolf M EMBO Rep. 2019 Mar 21. pii: embr.201846340. doi: 10.15252/embr.201846340. PMID:30898768<ref>PMID:30898768</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ya6" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Flagellin 3D structures|Flagellin 3D structures]]
*[[Flagellin 3D structures|Flagellin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Metja]]
[[Category: Methanocaldococcus jannaschii DSM 2661]]
[[Category: Meshcheryakov, V A]]
[[Category: Meshcheryakov VA]]
[[Category: Wolf, M]]
[[Category: Wolf M]]
[[Category: Archaea]]
[[Category: Flagellin]]
[[Category: Flagellum]]
[[Category: Structural protein]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/w/5ya6"