1hf2

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[[Image:1hf2.png|left|200px]]
 
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==Crystal structure of the bacterial cell-division inhibitor MinC from T. maritima==
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The line below this paragraph, containing "STRUCTURE_1hf2", creates the "Structure Box" on the page.
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<StructureSection load='1hf2' size='340' side='right'caption='[[1hf2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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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'>[[1hf2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HF2 FirstGlance]. <br>
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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]] 2.2&#8491;</td></tr>
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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=1hf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hf2 OCA], [https://pdbe.org/1hf2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hf2 RCSB], [https://www.ebi.ac.uk/pdbsum/1hf2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hf2 ProSAT]</span></td></tr>
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{{STRUCTURE_1hf2| PDB=1hf2 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MINC_THEMA MINC_THEMA] Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization (By similarity).
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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/hf/1hf2_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=1hf2 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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Bacterial cell division requires accurate selection of the middle of the cell, where the bacterial tubulin homologue FtsZ polymerizes into a ring structure. In Escherichia coli, site selection is dependent on MinC, MinD and MINE: MinC acts, with MinD, to inhibit division at sites other than the midcell by directly interacting with FTSZ: Here we report the crystal structure to 2.2 A of MinC from Thermotoga maritima. MinC consists of two domains separated by a short linker. The C-terminal domain is a right-handed beta-helix and is involved in dimer formation. The crystals contain two different MinC dimers, demonstrating flexibility in the linker region. The two-domain architecture and dimerization of MinC can be rationalized with a model of cell division inhibition. MinC does not act like SulA, which affects the GTPase activity of FtsZ, and the model can explain how MinC would select for the FtsZ polymer rather than the monomer.
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===CRYSTAL STRUCTURE OF THE BACTERIAL CELL-DIVISION INHIBITOR MINC FROM T. MARITIMA===
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Crystal structure of the bacterial cell division inhibitor MinC.,Cordell SC, Anderson RE, Lowe J EMBO J. 2001 May 15;20(10):2454-61. PMID:11350934<ref>PMID:11350934</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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The line below this paragraph, {{ABSTRACT_PUBMED_11350934}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1hf2" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11350934 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11350934}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1HF2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HF2 OCA].
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==Reference==
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Crystal structure of the bacterial cell division inhibitor MinC., Cordell SC, Anderson RE, Lowe J, EMBO J. 2001 May 15;20(10):2454-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11350934 11350934]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Anderson, R E.]]
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[[Category: Anderson RE]]
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[[Category: Cordell, S C.]]
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[[Category: Cordell SC]]
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[[Category: Lowe, J.]]
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[[Category: Lowe J]]
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[[Category: Bacterial cell division]]
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[[Category: Beta helix]]
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[[Category: Ftsz]]
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[[Category: Septum]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:06:03 2008''
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Current revision

Crystal structure of the bacterial cell-division inhibitor MinC from T. maritima

PDB ID 1hf2

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