3dpb: Difference between revisions

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New page: '''Unreleased structure''' The entry 3dpb is ON HOLD Authors: Fooks, L.J., Yu, X., Moslehi-Mohebi, E., Tischenko, V., Knight, S.D., MacIntyre, S., Zavialov, A.V. Description: Crystal s...
 
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'''Unreleased structure'''


The entry 3dpb is ON HOLD
==Crystal structure of the complex of the Caf1M chaperone with the mini-fiber of two Caf1 subunits (Caf1:Caf1), carrying the Ala9Val, Ala11Val, and Leu13Val mutations in the Gd donor strand==
 
<StructureSection load='3dpb' size='340' side='right'caption='[[3dpb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
Authors: Fooks, L.J., Yu, X., Moslehi-Mohebi, E., Tischenko, V., Knight, S.D., MacIntyre, S., Zavialov, A.V.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3dpb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DPB FirstGlance]. <br>
Description: Crystal structure of the complex of the Caf1M chaperone with the mini-fiber of two Caf1 subunits (Caf1:Caf1), carrying the Ala9Val, Ala11Val, and Leu13Val mutations in the Gd donor strand
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=3dpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dpb OCA], [https://pdbe.org/3dpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dpb RCSB], [https://www.ebi.ac.uk/pdbsum/3dpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dpb ProSAT]</span></td></tr>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 23 12:16:05 2008''
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAF1M_YERPE CAF1M_YERPE] Has a stimulatory role for the envelope antigen F1 secretion. It seems to interact with the subunit polypeptide and to prevent it from digestion by a protease.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/3dpb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=3dpb ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Yersinia pestis]]
[[Category: Fooks LJ]]
[[Category: Knight SD]]
[[Category: MacIntyre S]]
[[Category: Moslehi-Mohebi E]]
[[Category: Tischenko V]]
[[Category: Yu X]]
[[Category: Zavialov AV]]

Latest revision as of 04:43, 21 November 2024

Crystal structure of the complex of the Caf1M chaperone with the mini-fiber of two Caf1 subunits (Caf1:Caf1), carrying the Ala9Val, Ala11Val, and Leu13Val mutations in the Gd donor strandCrystal structure of the complex of the Caf1M chaperone with the mini-fiber of two Caf1 subunits (Caf1:Caf1), carrying the Ala9Val, Ala11Val, and Leu13Val mutations in the Gd donor strand

Structural highlights

3dpb is a 3 chain structure with sequence from Yersinia pestis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAF1M_YERPE Has a stimulatory role for the envelope antigen F1 secretion. It seems to interact with the subunit polypeptide and to prevent it from digestion by a protease.

Evolutionary Conservation

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

3dpb, resolution 2.20Å

Drag the structure with the mouse to rotate

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