3myd: Difference between revisions

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==Structure of the Cytoplasmic domain of FlhA from Helicobacter pylori==
==Structure of the Cytoplasmic domain of FlhA from Helicobacter pylori==
<StructureSection load='3myd' size='340' side='right' caption='[[3myd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3myd' size='340' side='right' caption='[[3myd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3myd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MYD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MYD FirstGlance]. <br>
<table><tr><td colspan='2'>[[3myd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MYD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MYD FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flbA, flhA, HP1041, jhp_0383 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori])</td></tr>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flbA, flhA, HP1041, jhp_0383 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</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=3myd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3myd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3myd RCSB], [http://www.ebi.ac.uk/pdbsum/3myd PDBsum]</span></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=3myd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3myd OCA], [http://pdbe.org/3myd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3myd RCSB], [http://www.ebi.ac.uk/pdbsum/3myd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3myd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=3myd ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3myd" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Helicobacter pylori]]
[[Category: Atcc 43504]]
[[Category: Jia, Y]]
[[Category: Jia, Y]]
[[Category: Moore, S A]]
[[Category: Moore, S A]]

Revision as of 16:49, 5 August 2016

Structure of the Cytoplasmic domain of FlhA from Helicobacter pyloriStructure of the Cytoplasmic domain of FlhA from Helicobacter pylori

Structural highlights

3myd is a 1 chain structure with sequence from Atcc 43504. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:flbA, flhA, HP1041, jhp_0383 (ATCC 43504)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FLHA_HELPJ] Involved in the export of flagellum proteins.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Using x-ray crystallography we have determined the structure of the cytoplasmic fragment (residues 384-732) of the flagellum secretion system protein FlhA from Helicobacter pylori at 2.4-A resolution (r = 0.224; R(free) = 0.263). FlhA proteins and their type III secretion homologues contain an N-terminal integral membrane domain (residues 1-350), a linker segment, and a globular C-terminal cytoplasmic region. The tertiary structure of the cytoplasmic fragment contains a thioredoxin-like domain, an RNA recognition motif-like domain inserted within the thioredoxin-fold, a helical domain, and a C-terminal beta/alpha domain. Inter-domain contacts are extensive and the H. pylori FlhA structure appears to be in a closed conformation where the C-terminal domain closes against the RNA recognition motif-fold domain. Highly conserved surface residues in FlhA proteins are concentrated on a narrow surface strip comprising the thioredoxin-like and helical domains, possibly close to the export channel opening. The conformation of the FlhA N-terminal linker segment suggests a likely orientation for the FlhA cytoplasmic fragment relative to the membrane-embedded export pore. Comparison with the recently published structures of the Salmonella FlhA cytoplasmic fragment and its type III secretion counterpart InvA highlight a conformational change where the C-terminal beta/alpha domain in H. pylori FlhA moves 15 A relative to Salmonella FlhA. The conformational change is complex but primarily involves hinge-like movements of the helical and C-terminal domains. Interpretation of previous mutational screens suggest that the C-terminal domain of FlhA(C) plays a regulatory role in substrate class switching in flagellum export.

Structure of the cytoplasmic domain of the flagellar secretion apparatus component FlhA from Helicobacter pylori.,Moore SA, Jia Y J Biol Chem. 2010 Jul 2;285(27):21060-9. Epub 2010 May 4. PMID:20442410[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Moore SA, Jia Y. Structure of the cytoplasmic domain of the flagellar secretion apparatus component FlhA from Helicobacter pylori. J Biol Chem. 2010 Jul 2;285(27):21060-9. Epub 2010 May 4. PMID:20442410 doi:10.1074/jbc.M110.119412

3myd, resolution 2.40Å

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OCA