3hj6: Difference between revisions

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[[Image:3hj6.png|left|200px]]


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==Structure of Halothermothrix orenii fructokinase (FRK)==
The line below this paragraph, containing "STRUCTURE_3hj6", creates the "Structure Box" on the page.
<StructureSection load='3hj6' size='340' side='right'caption='[[3hj6]], [[Resolution|resolution]] 2.80&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'>[[3hj6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Halothermothrix_orenii_H_168 Halothermothrix orenii H 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HJ6 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]] 2.8&#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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
{{STRUCTURE_3hj6|  PDB=3hj6  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hj6 OCA], [https://pdbe.org/3hj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hj6 RCSB], [https://www.ebi.ac.uk/pdbsum/3hj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hj6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B8CZ52_HALOH B8CZ52_HALOH]
== 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/hj/3hj6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3hj6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fructokinase (FRK; EC 2.7.1.4) catalyzes the phosphorylation of d-fructose to d-fructose 6-phosphate (F6P). This irreversible and near rate-limiting step is a central and regulatory process in plants and bacteria, which channels fructose into a metabolically active state for glycolysis. Towards understanding the mechanism of FRK, here we report the crystal structure of a FRK homolog from a thermohalophilic bacterium Halothermothrixorenii (Hore_18220 in sequence databases). The structure of the Hore_18220 protein reveals a catalytic domain with a Rossmann-like fold and a beta-sheet "lid" for dimerization. Based on comparison of Hore_18220 to structures of related proteins, we propose its mechanism of action, in which the lid serves to regulate access to the substrate binding sites. Close relationship of Hore_18220 and plant FRK enzymes allows us to propose a model for the structure and function of FRKs.


===Structure of Halothermothrix orenii fructokinase (FRK)===
Crystal structure of a fructokinase homolog from Halothermothrix orenii.,Chua TK, Seetharaman J, Kasprzak JM, Ng C, Patel BK, Love C, Bujnicki JM, Sivaraman J J Struct Biol. 2010 Sep;171(3):397-401. Epub 2010 May 21. PMID:20493950<ref>PMID:20493950</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3hj6" style="background-color:#fffaf0;"></div>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_20493950}}, adds the Publication Abstract to the page
*[[Fructokinase|Fructokinase]]
(as it appears on PubMed at http://www.pubmed.gov), where 20493950 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_20493950}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Halothermothrix orenii H 168]]
[[3hj6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Halothermothrix_orenii Halothermothrix orenii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJ6 OCA].
[[Category: Large Structures]]
 
[[Category: Bujnicki JM]]
==Reference==
[[Category: Chua TK]]
<ref group="xtra">PMID:20493950</ref><references group="xtra"/>
[[Category: Kasprzak JM]]
[[Category: Fructokinase]]
[[Category: Love C]]
[[Category: Halothermothrix orenii]]
[[Category: Ng C]]
[[Category: Bujnicki, J M.]]
[[Category: Patel BK]]
[[Category: Chua, T K.]]
[[Category: Seetharaman J]]
[[Category: Kasprzak, J M.]]
[[Category: Sivaraman J]]
[[Category: Love, C.]]
[[Category: Ng, C.]]
[[Category: Patel, B K.]]
[[Category: Seetharaman, J.]]
[[Category: Sivaraman, J.]]
[[Category: Carbohydrate metabolism]]
[[Category: Fructokinase]]
[[Category: Fructose]]
[[Category: Kinase]]
[[Category: Transferase]]

Latest revision as of 12:14, 30 October 2024

Structure of Halothermothrix orenii fructokinase (FRK)Structure of Halothermothrix orenii fructokinase (FRK)

Structural highlights

3hj6 is a 2 chain structure with sequence from Halothermothrix orenii H 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B8CZ52_HALOH

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

Fructokinase (FRK; EC 2.7.1.4) catalyzes the phosphorylation of d-fructose to d-fructose 6-phosphate (F6P). This irreversible and near rate-limiting step is a central and regulatory process in plants and bacteria, which channels fructose into a metabolically active state for glycolysis. Towards understanding the mechanism of FRK, here we report the crystal structure of a FRK homolog from a thermohalophilic bacterium Halothermothrixorenii (Hore_18220 in sequence databases). The structure of the Hore_18220 protein reveals a catalytic domain with a Rossmann-like fold and a beta-sheet "lid" for dimerization. Based on comparison of Hore_18220 to structures of related proteins, we propose its mechanism of action, in which the lid serves to regulate access to the substrate binding sites. Close relationship of Hore_18220 and plant FRK enzymes allows us to propose a model for the structure and function of FRKs.

Crystal structure of a fructokinase homolog from Halothermothrix orenii.,Chua TK, Seetharaman J, Kasprzak JM, Ng C, Patel BK, Love C, Bujnicki JM, Sivaraman J J Struct Biol. 2010 Sep;171(3):397-401. Epub 2010 May 21. PMID:20493950[1]

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

See Also

References

  1. ↑ Chua TK, Seetharaman J, Kasprzak JM, Ng C, Patel BK, Love C, Bujnicki JM, Sivaraman J. Crystal structure of a fructokinase homolog from Halothermothrix orenii. J Struct Biol. 2010 Sep;171(3):397-401. Epub 2010 May 21. PMID:20493950 doi:10.1016/j.jsb.2010.05.007

3hj6, resolution 2.80Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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