1b67

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(New page: 200px<br /><applet load="1b67" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b67, resolution 1.48&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1b67.gif|left|200px]]<br /><applet load="1b67" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1b67, resolution 1.48&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE HISTONE HMFA FROM METHANOTHERMUS FERVIDUS'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE HISTONE HMFA FROM METHANOTHERMUS FERVIDUS==
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The hyperthermophilic archaeon Methanothermus fervidus contains two small, basic proteins, HMfA (68 amino acid residues) and HMfB (69 residues) that, share a common ancestry with the eukaryal nucleosome core histones H2A, H2B, H3, and H4. HMfA and HMfB have sequences that differ at 11 locations, they have different structural stabilities, and the complexes that they, form with DNA have different electrophoretic mobilities. Here, crystal, structures are documented for recombinant (r) HMfA at a resolution of 1.55, A refined to a crystallographic R-value of 19.8 % (tetragonal form) and at, 1.48 A refined to a R-value of 18.8 % (orthorhombic form), and for rHMfB, at 1.9 A refined to a R-value of 18.0 %. The rHMfA and rHMfB monomers have, structures that are just histone folds in which a long central alpha-helix, (alpha2; 29 residues) is separated from shorter N-terminal (alpha1; 11, residues) and C-terminal (alpha3; 10 residues) alpha-helices by two loops, (L1 and L2; both 6 residues). Within L1 and L2, three adjacent residues, are in extended (beta) conformation. rHMfA and rHMfB assemble into, homodimers, with the alpha2 helices anti-parallel aligned and crossing at, an angle of close to 35 degrees, and with hydrogen bonds formed between, the extended, parallel regions of L1 and L2 resulting in short, beta-ladders. Dimerization creates a novel N-terminal structure that, contains four proline residues, two from each monomer. As prolines are, present at these positions in all archaeal histone sequences, this, proline-tetrad structure is likely to be a common feature of all archaeal, histone dimers. Almost all residues that participate in monomer-monomer, interactions are conserved in HMfA and HMfB, consistent with the ability, of these monomers to form both homodimers and (HMfA+HMfB) heterodimers., Differences in side-chain interactions that result from non-conservative, residue differences in HMfA and HMfB are identified, and the structure of, a (rHMfA)(2)-DNA complex is presented based on the structures documented, here and modeled by homology to histone-DNA interactions in the eukaryal, nucleosome.
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<StructureSection load='1b67' size='340' side='right'caption='[[1b67]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1b67]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermus_fervidus Methanothermus fervidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B67 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]] 1.48&#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=SO4:SULFATE+ION'>SO4</scene></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=1b67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b67 OCA], [https://pdbe.org/1b67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b67 RCSB], [https://www.ebi.ac.uk/pdbsum/1b67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b67 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HMFA_METFE HMFA_METFE] Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation.
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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/b6/1b67_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=1b67 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1B67 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermus_fervidus Methanothermus fervidus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B67 OCA].
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*[[Histone 3D structures|Histone 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures of recombinant histones HMfA and HMfB from the hyperthermophilic archaeon Methanothermus fervidus., Decanniere K, Babu AM, Sandman K, Reeve JN, Heinemann U, J Mol Biol. 2000 Oct 13;303(1):35-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11021968 11021968]
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[[Category: Large Structures]]
[[Category: Methanothermus fervidus]]
[[Category: Methanothermus fervidus]]
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[[Category: Single protein]]
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[[Category: Decanniere K]]
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[[Category: Decanniere, K.]]
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[[Category: Heinemann U]]
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[[Category: Heinemann, U.]]
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[[Category: Reeve JN]]
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[[Category: Reeve, J.N.]]
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[[Category: Sandman K]]
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[[Category: Sandman, K.]]
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[[Category: SO4]]
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[[Category: histone]]
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[[Category: hmf1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:23:40 2007''
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Current revision

CRYSTAL STRUCTURE OF THE HISTONE HMFA FROM METHANOTHERMUS FERVIDUS

PDB ID 1b67

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