2c0f: Difference between revisions

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==STRUCTURE OF WIND Y53F MUTANT==
 
<StructureSection load='2c0f' size='340' side='right' caption='[[2c0f]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
==Structure of Wind Y53F mutant==
<StructureSection load='2c0f' size='340' side='right'caption='[[2c0f]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2c0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C0F FirstGlance]. <br>
<table><tr><td colspan='2'>[[2c0f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C0F FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ovn|1ovn]], [[2c0e|2c0e]], [[2c0g|2c0g]], [[2c1y|2c1y]]</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]] 2.28&#8491;</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c0f RCSB], [http://www.ebi.ac.uk/pdbsum/2c0f PDBsum]</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=2c0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0f OCA], [https://pdbe.org/2c0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c0f RCSB], [https://www.ebi.ac.uk/pdbsum/2c0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c0f ProSAT]</span></td></tr>
<table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/WBL_DROME WBL_DROME] Probable chaperone protein involved in dorsoventral axis patterning in early embryos. Probably acts by folding and targeting pipe (pip) into the Golgi.<ref>PMID:9568717</ref> <ref>PMID:11076773</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c0/2c0f_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c0/2c0f_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <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=2c0f 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 2c0f" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Barnewitz, K.]]
[[Category: Large Structures]]
[[Category: Ferrari, D M.]]
[[Category: Barnewitz K]]
[[Category: Guo, C.]]
[[Category: Ferrari DM]]
[[Category: Ma, Q.]]
[[Category: Guo C]]
[[Category: Sevvana, M.]]
[[Category: Ma Q]]
[[Category: Sheldrick, G M.]]
[[Category: Sevvana M]]
[[Category: Soling, H D.]]
[[Category: Sheldrick GM]]
[[Category: Chaperone]]
[[Category: Soling H-D]]
[[Category: Developmental protein]]
[[Category: Dorsal-ventral patterning]]
[[Category: Endoplasmic reticulum]]
[[Category: Pdi]]
[[Category: Pdi-dbeta]]
[[Category: Pipe]]
[[Category: Protein disulfide isomerase]]
[[Category: Wind]]
[[Category: Wind mutant]]
[[Category: Windbeutel]]

Latest revision as of 17:00, 13 December 2023

Structure of Wind Y53F mutantStructure of Wind Y53F mutant

Structural highlights

2c0f is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.28Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

WBL_DROME Probable chaperone protein involved in dorsoventral axis patterning in early embryos. Probably acts by folding and targeting pipe (pip) into the Golgi.[1] [2]

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

The structures of the PDI-related protein Wind (with a C-terminal His(6) tag) and the mutants Y53S, Y53F and Y55K have been determined and compared with the wild-type structure with the His(6) tag at the N-terminus. All five structures show the same mode of dimerization, showing that this was not an artefact introduced by the nearby N-terminal His(6) tag and suggesting that this dimer may also be the biologically active form. Although the mutants Y53S and Y55K completely abrogate transport of the protein Pipe (which appears to be the primary function of Wind in the cell), only subtle differences can be seen in the putative Pipe-binding region. The Pipe binding in the active forms appears to involve hydrophobic interactions between aromatic systems, whereas the inactive mutants may be able to bind more strongly with the help of hydrogen bonds, which could disturb the delicate equilibrium required for effective Pipe transport.

Structural elucidation of the PDI-related chaperone Wind with the help of mutants.,Sevvana M, Biadene M, Ma Q, Guo C, Soling HD, Sheldrick GM, Ferrari DM Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):589-94. Epub 2006, May 12. PMID:16699185[3]

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

References

  1. Nilson LA, Schupbach T. Localized requirements for windbeutel and pipe reveal a dorsoventral prepattern within the follicular epithelium of the Drosophila ovary. Cell. 1998 Apr 17;93(2):253-62. PMID:9568717
  2. Sen J, Goltz JS, Konsolaki M, Schupbach T, Stein D. Windbeutel is required for function and correct subcellular localization of the Drosophila patterning protein Pipe. Development. 2000 Dec;127(24):5541-50. PMID:11076773
  3. Sevvana M, Biadene M, Ma Q, Guo C, Soling HD, Sheldrick GM, Ferrari DM. Structural elucidation of the PDI-related chaperone Wind with the help of mutants. Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):589-94. Epub 2006, May 12. PMID:16699185 doi:10.1107/S0907444906010456

2c0f, resolution 2.28Å

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