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{{STRUCTURE_1hta|  PDB=1hta  |  SCENE=  }}
===CRYSTAL STRUCTURE OF THE HISTONE HMFA FROM METHANOTHERMUS FERVIDUS===
{{ABSTRACT_PUBMED_11021968}}


==About this Structure==
==CRYSTAL STRUCTURE OF THE HISTONE HMFA FROM METHANOTHERMUS FERVIDUS==
[[1hta]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanothermus_fervidus Methanothermus fervidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTA OCA].  
<StructureSection load='1hta' size='340' side='right'caption='[[1hta]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hta]] is a 1 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=1HTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hta OCA], [https://pdbe.org/1hta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hta RCSB], [https://www.ebi.ac.uk/pdbsum/1hta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hta ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/1hta_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1hta ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Archaeal Histones|Archaeal Histones]]
*[[Histone 3D structures|Histone 3D structures]]
*[[Histone|Histone]]
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
<ref group="xtra">PMID:011021968</ref><ref group="xtra">PMID:015048824</ref><references group="xtra"/>
[[Category: Methanothermus fervidus]]
[[Category: Methanothermus fervidus]]
[[Category: Decanniere, K.]]
[[Category: Decanniere K]]
[[Category: Heinemann, U.]]
[[Category: Heinemann U]]
[[Category: Reeve, J N.]]
[[Category: Reeve JN]]
[[Category: Sandman, K.]]
[[Category: Sandman K]]
[[Category: Histone]]

Latest revision as of 10:30, 7 February 2024

CRYSTAL STRUCTURE OF THE HISTONE HMFA FROM METHANOTHERMUS FERVIDUSCRYSTAL STRUCTURE OF THE HISTONE HMFA FROM METHANOTHERMUS FERVIDUS

Structural highlights

1hta is a 1 chain structure with sequence from Methanothermus fervidus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.55Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1hta, resolution 1.55Å

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