2wuj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2wuj" [edit=sysop:move=sysop])
Current revision (10:17, 9 May 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2wuj.png|left|200px]]
 
-
<!--
+
==DivIVA N-terminal domain==
-
The line below this paragraph, containing "STRUCTURE_2wuj", creates the "Structure Box" on the page.
+
<StructureSection load='2wuj' size='340' side='right'caption='[[2wuj]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2wuj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WUJ FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#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=2wuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wuj OCA], [https://pdbe.org/2wuj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wuj RCSB], [https://www.ebi.ac.uk/pdbsum/2wuj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wuj ProSAT]</span></td></tr>
-
{{STRUCTURE_2wuj| PDB=2wuj | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/DIV4A_BACSU DIV4A_BACSU] May act as a pilot protein, directing MinCD to the polar septation sites or by inhibiting MinCD at the midcell site of division. Required for polar localization of the chromosome during sporulation.<ref>PMID:9045828</ref> <ref>PMID:9219999</ref>
 +
== 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/wu/2wuj_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2wuj ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
DivIVA is a conserved protein in Gram-positive bacteria that localizes at the poles and division sites, presumably through direct sensing of membrane curvature. DivIVA functions as a scaffold and is vital for septum site selection during vegetative growth and chromosome anchoring during sporulation. DivIVA deletion causes filamentous growth in Bacillus subtilis, whereas overexpression causes hyphal branching in Streptomyces coelicolor. We have determined the crystal structure of the N-terminal (Nt) domain of DivIVA, and show that it forms a parallel coiled-coil. It is capped with two unique crossed and intertwined loops, exposing hydrophobic and positively charged residues that we show here are essential for membrane binding. An intragenic suppressor introducing a positive charge restores membrane binding after mutating the hydrophobic residues. We propose that the hydrophobic residues insert into the membrane and that the positively charged residues bind to the membrane surface. A low-resolution crystal structure of the C-terminal (Ct) domain displays a curved tetramer made from two parallel coiled-coils. The Nt and Ct parts were then merged into a model of the full length, 30 nm long DivIVA protein.
-
===DIVIVA N-TERMINAL DOMAIN===
+
Features critical for membrane binding revealed by DivIVA crystal structure.,Oliva MA, Halbedel S, Freund SM, Dutow P, Leonard TA, Veprintsev DB, Hamoen LW, Lowe J EMBO J. 2010 Jun 16;29(12):1988-2001. Epub 2010 May 25. PMID:20502438<ref>PMID:20502438</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_20502438}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2wuj" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 20502438 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_20502438}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
[[2wuj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WUJ OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:20502438</ref><references group="xtra"/>
+
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
-
[[Category: Leonard, T A.]]
+
[[Category: Large Structures]]
-
[[Category: Lowe, J.]]
+
[[Category: Leonard TA]]
-
[[Category: Oliva, M A.]]
+
[[Category: Lowe J]]
-
[[Category: Bacterial cell division]]
+
[[Category: Oliva MA]]
-
[[Category: Cell cycle]]
+
-
[[Category: Septation]]
+
-
[[Category: Sporulation]]
+

Current revision

DivIVA N-terminal domain

PDB ID 2wuj

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools