1mul

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[[Image:1mul.gif|left|200px]]
 
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==Crystal structure of the E. coli HU alpha2 protein==
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The line below this paragraph, containing "STRUCTURE_1mul", creates the "Structure Box" on the page.
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<StructureSection load='1mul' size='340' side='right'caption='[[1mul]], [[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'>[[1mul]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MUL 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mul OCA], [https://pdbe.org/1mul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mul RCSB], [https://www.ebi.ac.uk/pdbsum/1mul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mul ProSAT]</span></td></tr>
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{{STRUCTURE_1mul| PDB=1mul | SCENE= }}
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</table>
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== Function ==
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'''Crystal structure of the E. coli HU alpha2 protein'''
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[https://www.uniprot.org/uniprot/DBHA_ECOLI DBHA_ECOLI] Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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The Escherichia coli histone-like HU protein pool is composed of three dimeric forms: two homodimers, EcHUalpha(2) and EcHUbeta(2), and a heterodimer, EcHUalphabeta. The relative abundance of these dimeric forms varies during cell growth and in response to environmental changes, suggesting that each dimer plays different physiological roles. Here, differential scanning calorimetry and circular dichroism (CD) were used to study the thermal stability of the three E.coli HU dimers and show that each of them has its own thermodynamic signature. Unlike the other HU proteins studied so far, which melt through a single step (N(2)&lt;--&gt;2D), this present thermodynamic study shows that the three E.coli dimers melt according to a two-step mechanism (N(2)&lt;--&gt;I(2)&lt;--&gt;2D). The native dimer, N(2), melts partially into a dimeric intermediate, I(2), which in turn yields the unfolded monomers, D. In addition, the crystal structure of the EcHUalpha(2) dimer has been solved. Comparative thermodynamic and structural analysis between EcHUalpha(2) and the HU homodimer from Bacillus stearothermophilus suggests that the E.coli dimer is constituted by two subdomains of different energetic properties. The CD study indicates that the intermediate, I(2), corresponds to an HU dimer having partly lost its alpha-helices. The partially unfolded dimer I(2) is unable to complex with high-affinity, single-stranded break-containing DNA. These structural, thermodynamic and functional results suggest that the N(2)&lt;--&gt;I(2) equilibrium plays a central role in the physiology of E.coli HU. The I(2) molecular species seems to be the EcHUbeta(2) preferential conformation, possibly related to its role in the E.coli cold-shock adaptation. Besides, I(2) might be required in E.coli for the HU chain exchange, which allows the heterodimer formation from homodimers.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1mul_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1MUL is a [[Single protein]] structure of 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=1MUL OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=1mul ConSurf].
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Evidence of a thermal unfolding dimeric intermediate for the Escherichia coli histone-like HU proteins: thermodynamics and structure., Ramstein J, Hervouet N, Coste F, Zelwer C, Oberto J, Castaing B, J Mol Biol. 2003 Aug 1;331(1):101-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12875839 12875839]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Castaing, B.]]
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[[Category: Castaing B]]
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[[Category: Coste, F.]]
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[[Category: Coste F]]
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[[Category: Hervouet, N.]]
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[[Category: Hervouet N]]
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[[Category: Oberto, J.]]
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[[Category: Oberto J]]
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[[Category: Ramstein, J.]]
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[[Category: Ramstein J]]
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[[Category: Zelwer, C.]]
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[[Category: Zelwer C]]
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[[Category: Histone-like]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:44:21 2008''
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Current revision

Crystal structure of the E. coli HU alpha2 protein

PDB ID 1mul

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