2wmm

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[[Image:2wmm.png|left|200px]]
 
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==Crystal structure of the hinge domain of MukB==
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The line below this paragraph, containing "STRUCTURE_2wmm", creates the "Structure Box" on the page.
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<StructureSection load='2wmm' size='340' side='right'caption='[[2wmm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2wmm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WMM FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLT:D-MALATE'>MLT</scene></td></tr>
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{{STRUCTURE_2wmm| PDB=2wmm | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wmm OCA], [https://pdbe.org/2wmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wmm RCSB], [https://www.ebi.ac.uk/pdbsum/2wmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wmm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MUKB_ECOLI MUKB_ECOLI] 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 organizes and compacts chromosomes. May achieve or facilitate chromosome segregation by condensation of DNA from both sides of a centrally located replisome during cell division. Stimulates both DNA relaxation and to a lesser extent decatenation activity of topoisomerase IV.<ref>PMID:20921377</ref> <ref>PMID:10660686</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wm/2wmm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2wmm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structural maintenance of chromosomes (SMC) family proteins are commonly found in the multiprotein complexes involved in chromosome organization, including chromosome condensation and sister chromatid cohesion. These proteins are characterized by forming a V-shaped homo- or heterodimeric structure with two long coiled-coil arms having two ATPase head domains at the distal ends. The hinge domain, located in the middle of the coiled coil, forms the dimer interface. In addition to being the dimerization module, SMC hinges appear to play other roles, including the gateway function for DNA entry into the cohesin complex. Herein, we report the homodimeric structure of the hinge domain of Escherichia coli MukB, which forms a prokaryotic condensin complex with two non-SMC subunits, MukE and MukF. In contrast with SMC hinge of Thermotoga maritima which has a sizable central hole at the dimer interface, MukB hinge forms a constricted dimer interface lacking a hole. Under our assay conditions, MukB hinge does not interact with DNA in accordance with the absence of a notable positively charged surface patch. The function of MukB hinge appears to be limited to dimerization of two copies of MukB molecules. Proteins 2010. (c) 2009 Wiley-Liss, Inc.
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===CRYSTAL STRUCTURE OF THE HINGE DOMAIN OF MUKB===
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Crystal structure of the MukB hinge domain with coiled-coil stretches and its functional implications.,Ku B, Lim JH, Shin HC, Shin SY, Oh BH Proteins. 2009 Nov 24. PMID:20034111<ref>PMID:20034111</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2wmm" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20034111}}, adds the Publication Abstract to the page
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*[[Condensin|Condensin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20034111 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20034111}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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[[2wmm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WMM OCA].
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[[Category: Large Structures]]
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[[Category: Ku B]]
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==Reference==
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[[Category: Oh B-H]]
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<ref group="xtra">PMID:020034111</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
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[[Category: Ku, B.]]
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[[Category: Oh, B H.]]
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[[Category: Atp-binding]]
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[[Category: Cell cycle]]
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[[Category: Cell division]]
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[[Category: Chromosome partition]]
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[[Category: Condensin]]
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[[Category: Dna condensation]]
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[[Category: Dna-binding]]
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[[Category: Hinge]]
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[[Category: Mukb]]
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[[Category: Mukbef]]
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[[Category: Nucleotide-binding]]
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[[Category: Smc]]
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Current revision

Crystal structure of the hinge domain of MukB

PDB ID 2wmm

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