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3euj

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Revision as of 09:20, 25 October 2017

Crystal structure of MukE-MukF(residues 292-443)-MukB(head domain)-ATPgammaS complex, symmetric dimer

Structural highlights

3euj is a 2 chain structure with sequence from "bacillus_ulceris_cancrosi"_kruse_1896 "bacillus ulceris cancrosi" kruse 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	3euh, 3euk
Gene:	mukB, HD_1582 ("Bacillus ulceris cancrosi" Kruse 1896), mukF, HD_1585 ("Bacillus ulceris cancrosi" Kruse 1896)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MUKB_HAEDU] Plays a central role in chromosome condensation, segregation and cell cycle progression. Functions as a homodimer, which is essential for chromosome partition. Involved in negative DNA supercoiling in vivo, and by this means organize and compact chromosomes. May achieve or facilitate chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division (By similarity). [MUKF_HAEDU] Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Not required for mini-F plasmid partitioning. Probably acts via its interaction with MukB and MukE. Overexpression results in anucleate cells. It has a calcium binding activity (By similarity).

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

Condensins are key mediators of chromosome condensation across organisms. Like other condensins, the bacterial MukBEF condensin complex consists of an SMC family protein dimer containing two ATPase head domains, MukB, and two interacting subunits, MukE and MukF. We report complete structural views of the intersubunit interactions of this condensin along with ensuing studies that reveal a role for the ATPase activity of MukB. MukE and MukF together form an elongated dimeric frame, and MukF's C-terminal winged-helix domains (C-WHDs) bind MukB heads to constitute closed ring-like structures. Surprisingly, one of the two bound C-WHDs is forced to detach upon ATP-mediated engagement of MukB heads. This detachment reaction depends on the linker segment preceding the C-WHD, and mutations on the linker restrict cell growth. Thus ATP-dependent transient disruption of the MukB-MukF interaction, which creates openings in condensin ring structures, is likely to be a critical feature of the functional mechanism of condensins.

Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions.,Woo JS, Lim JH, Shin HC, Suh MK, Ku B, Lee KH, Joo K, Robinson H, Lee J, Park SY, Ha NC, Oh BH Cell. 2009 Jan 9;136(1):85-96. PMID:19135891^[1]

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

References

↑ Woo JS, Lim JH, Shin HC, Suh MK, Ku B, Lee KH, Joo K, Robinson H, Lee J, Park SY, Ha NC, Oh BH. Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions. Cell. 2009 Jan 9;136(1):85-96. PMID:19135891 doi:10.1016/j.cell.2008.10.050

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3euj"

@@ Line 3: / Line 3: @@
 <StructureSection load='3euj' size='340' side='right' caption='[[3euj]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3euj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EUJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3euj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_ulceris_cancrosi"_kruse_1896 "bacillus ulceris cancrosi" kruse 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EUJ FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3euh|3euh]], [[3euk|3euk]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mukB, HD_1582 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=730 "Bacillus ulceris cancrosi" Kruse 1896]), mukF, HD_1585 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=730 "Bacillus ulceris cancrosi" Kruse 1896])</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=3euj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3euj OCA], [http://pdbe.org/3euj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3euj RCSB], [http://www.ebi.ac.uk/pdbsum/3euj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3euj ProSAT]</span></td></tr>
 </table>
@@ Line 33: / Line 34: @@
 __TOC__
 </StructureSection>
+[[Category: Bacillus ulceris cancrosi kruse 1896]]
 [[Category: Lim, J H]]
 [[Category: Oh, B H]]

3euj

From Proteopedia

Revision as of 09:20, 25 October 2017

Crystal structure of MukE-MukF(residues 292-443)-MukB(head domain)-ATPgammaS complex, symmetric dimer

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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