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| | <StructureSection load='4wia' size='340' side='right'caption='[[4wia]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4wia' size='340' side='right'caption='[[4wia]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wia]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WIA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WIA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wia]] is a 3 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=4WIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WIA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4wia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wia OCA], [https://pdbe.org/4wia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wia RCSB], [https://www.ebi.ac.uk/pdbsum/4wia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wia ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flaH, MJ0899 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wia OCA], [http://pdbe.org/4wia PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wia RCSB], [http://www.ebi.ac.uk/pdbsum/4wia PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wia ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FLAH_METJA FLAH_METJA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </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: Atp-binding protein]]
| + | |
| - | [[Category: Flagella]]
| + | |
| Structural highlights
Function
FLAH_METJA
Publication Abstract from PubMed
Archaeal flagella are unique structures that share functional similarity with bacterial flagella, but are structurally related to bacterial type IV pili. The flagellar accessory protein FlaH is one of the conserved components of the archaeal motility system. However, its function is not clearly understood. Here, we present the 2.2 A resolution crystal structure of FlaH from the hyperthermophilic archaeon, Methanocaldococcus jannaschii. The protein has a characteristic RecA-like fold, which has been found previously both in archaea and bacteria. We show that FlaH binds to immobilized ATP-however, it lacks ATPase activity. Surface plasmon resonance analysis demonstrates that ATP affects the interaction between FlaH and the archaeal motor protein FlaI. In the presence of ATP, the FlaH-FlaI interaction becomes significantly weaker. A database search revealed similarity between FlaH and several DNA-binding proteins of the RecA superfamily. The closest structural homologs of FlaH are KaiC-like proteins, which are archaeal homologs of the circadian clock protein KaiC from cyanobacteria. We propose that one of the functions of FlaH may be the regulation of archaeal motor complex assembly.
Crystal structure of the flagellar accessory protein FlaH of Methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly.,Meshcheryakov VA, Wolf M Protein Sci. 2016 Jun;25(6):1147-55. doi: 10.1002/pro.2932. Epub 2016 May 1. PMID:27060465[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Meshcheryakov VA, Wolf M. Crystal structure of the flagellar accessory protein FlaH of Methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly. Protein Sci. 2016 Jun;25(6):1147-55. doi: 10.1002/pro.2932. Epub 2016 May 1. PMID:27060465 doi:http://dx.doi.org/10.1002/pro.2932
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