1hyq

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[[Image:1hyq.jpg|left|200px]]<br /><applet load="1hyq" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hyq, resolution 2.6&Aring;" />
 
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'''MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS'''<br />
 
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==Overview==
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==MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS==
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In bacterial cell division MinD plays a pivotal role, selecting the mid-cell over other sites. With MinC, MinD forms a non-specific inhibitor of division, that interacts with FtsZ. Specificity is provided by MinD's interaction with MinE at the mid-cell. We have solved the crystal structure of MinD-1 from Archaeoglobus fulgidus to 2.6 A by multiple anomalous dispersion. MinD is a classic nucleotide binding protein, related to nitrogenase iron proteins, which have a fold of a seven-stranded parallel beta-sheet, surrounded by alpha-helices. Although MinD, unlike the proteins it interacts with and those it is structurally related to, is a monomer, not a dimer.
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<StructureSection load='1hyq' size='340' side='right'caption='[[1hyq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1hyq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYQ FirstGlance]. <br>
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1HYQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYQ OCA].
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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]] 2.6&#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=1hyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyq OCA], [https://pdbe.org/1hyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hyq RCSB], [https://www.ebi.ac.uk/pdbsum/1hyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hyq ProSAT]</span></td></tr>
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==Reference==
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</table>
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Crystal structure of the bacterial cell division regulator MinD., Cordell SC, Lowe J, FEBS Lett. 2001 Mar 9;492(1-2):160-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11248256 11248256]
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== Function ==
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[https://www.uniprot.org/uniprot/O29562_ARCFU O29562_ARCFU]
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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/hy/1hyq_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=1hyq ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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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: ftsz]]
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[[Category: minc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:11 2008''
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Current revision

MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS

PDB ID 1hyq

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