2ibl: Difference between revisions

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[[Image:2ibl.png|left|200px]]


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==Crystal structure of a helper molecule (HT-mf-thromb) based on mini-fibritin (mf) crystal structure (pdb:1OX3).==
The line below this paragraph, containing "STRUCTURE_2ibl", creates the "Structure Box" on the page.
<StructureSection load='2ibl' size='340' side='right'caption='[[2ibl]], [[Resolution|resolution]] 1.32&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2ibl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_Ox2 Enterobacteria phage Ox2] and [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IBL FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.32&#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=2ibl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ibl OCA], [https://pdbe.org/2ibl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ibl RCSB], [https://www.ebi.ac.uk/pdbsum/2ibl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ibl ProSAT]</span></td></tr>
{{STRUCTURE_2ibl|  PDB=2ibl  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q38650_BPOX2 Q38650_BPOX2]
== 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/ib/2ibl_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=2ibl ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hantaviruses can cause hemorrhagic fever with a renal syndrome and hantavirus pulmonary syndrome when transmitted to humans. The nucleocapsid protein of hantaviruses encapsidates viral genomic RNA and associates with transcription and replication complexes. Both the amino and carboxy termini of the nucleocapsid protein had been predicted to form trimers prior to the formation of the ribonucleoprotein. Crystal structures of amino-terminal fragments of the nucleocapsid protein showed the formation of intramolecular antiparallel coiled coils, but not intermolecular trimers. Thus, the amino-terminal part of the nucleocapsid protein is probably insufficient to initiate the trimerization of the full-length molecule.


===Crystal structure of a helper molecule (HT-mf-thromb) based on mini-fibritin (mf) crystal structure (pdb:1OX3).===
The coiled-coil domain structure of the Sin Nombre virus nucleocapsid protein.,Boudko SP, Kuhn RJ, Rossmann MG J Mol Biol. 2007 Mar 9;366(5):1538-44. Epub 2006 Dec 23. PMID:17222867<ref>PMID:17222867</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ibl" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_17222867}}, adds the Publication Abstract to the page
*[[Fibritin|Fibritin]]
(as it appears on PubMed at http://www.pubmed.gov), where 17222867 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_17222867}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Enterobacteria phage Ox2]]
[[2ibl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Unidentified_phage Unidentified phage]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IBL OCA].
[[Category: Escherichia virus T4]]
 
[[Category: Large Structures]]
==Reference==
[[Category: Boudko SP]]
<ref group="xtra">PMID:17222867</ref><ref group="xtra">PMID:15165860</ref><references group="xtra"/>
[[Category: Rossmann MG]]
[[Category: Unidentified phage]]
[[Category: Boudko, S P.]]
[[Category: Rossmann, M G.]]
[[Category: Bacteriophage t4]]
[[Category: Chaperone]]
[[Category: Foldon]]
[[Category: Helper molecule]]
[[Category: Mini-fibritin]]
[[Category: Trimerization]]

Latest revision as of 13:08, 30 August 2023

Crystal structure of a helper molecule (HT-mf-thromb) based on mini-fibritin (mf) crystal structure (pdb:1OX3).Crystal structure of a helper molecule (HT-mf-thromb) based on mini-fibritin (mf) crystal structure (pdb:1OX3).

Structural highlights

2ibl is a 1 chain structure with sequence from Enterobacteria phage Ox2 and Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.32Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q38650_BPOX2

Evolutionary Conservation

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

Publication Abstract from PubMed

Hantaviruses can cause hemorrhagic fever with a renal syndrome and hantavirus pulmonary syndrome when transmitted to humans. The nucleocapsid protein of hantaviruses encapsidates viral genomic RNA and associates with transcription and replication complexes. Both the amino and carboxy termini of the nucleocapsid protein had been predicted to form trimers prior to the formation of the ribonucleoprotein. Crystal structures of amino-terminal fragments of the nucleocapsid protein showed the formation of intramolecular antiparallel coiled coils, but not intermolecular trimers. Thus, the amino-terminal part of the nucleocapsid protein is probably insufficient to initiate the trimerization of the full-length molecule.

The coiled-coil domain structure of the Sin Nombre virus nucleocapsid protein.,Boudko SP, Kuhn RJ, Rossmann MG J Mol Biol. 2007 Mar 9;366(5):1538-44. Epub 2006 Dec 23. PMID:17222867[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Boudko SP, Kuhn RJ, Rossmann MG. The coiled-coil domain structure of the Sin Nombre virus nucleocapsid protein. J Mol Biol. 2007 Mar 9;366(5):1538-44. Epub 2006 Dec 23. PMID:17222867 doi:10.1016/j.jmb.2006.12.046

2ibl, resolution 1.32Å

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OCA