1kzh: Difference between revisions

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{{Seed}}
[[Image:1kzh.png|left|200px]]


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==Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi==
The line below this paragraph, containing "STRUCTURE_1kzh", creates the "Structure Box" on the page.
<StructureSection load='1kzh' size='340' side='right'caption='[[1kzh]], [[Resolution|resolution]] 2.55&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'>[[1kzh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi Borreliella burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KZH 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]] 2.55&#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>
{{STRUCTURE_1kzh| PDB=1kzh |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kzh OCA], [https://pdbe.org/1kzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kzh RCSB], [https://www.ebi.ac.uk/pdbsum/1kzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kzh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PFP_BORBU PFP_BORBU] Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.[HAMAP-Rule:MF_01980]<ref>PMID:10545221</ref>
== 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/kz/1kzh_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=1kzh ConSurf].
<div style="clear:both"></div>


===Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi===
==See Also==
 
*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]]
 
== References ==
<!--
<references/>
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__TOC__
(as it appears on PubMed at http://www.pubmed.gov), where 12015149 is the PubMed ID number.
</StructureSection>
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[[Category: Borreliella burgdorferi]]
{{ABSTRACT_PUBMED_12015149}}
[[Category: Large Structures]]
 
[[Category: Moore SA]]
==About this Structure==
[[Category: Morgan HW]]
1KZH is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZH OCA].
[[Category: Roberson RS]]
 
[[Category: Ronimus RS]]
==Reference==
<ref group="xtra">PMID:12015149</ref><references group="xtra"/>
[[Category: Borrelia burgdorferi]]
[[Category: Diphosphate--fructose-6-phosphate 1-phosphotransferase]]
[[Category: Moore, S A.]]
[[Category: Morgan, H W.]]
[[Category: Roberson, R S.]]
[[Category: Ronimus, R S.]]
[[Category: Borrelia burgdorferi]]
[[Category: Phosphofructokinase]]
[[Category: Phosphotransferase]]
[[Category: Pyrophosphate]]
[[Category: Spirochete]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:40:54 2009''

Latest revision as of 16:26, 13 March 2024

Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferiStructure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi

Structural highlights

1kzh is a 2 chain structure with sequence from Borreliella burgdorferi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.55Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PFP_BORBU Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.[HAMAP-Rule:MF_01980][1]

Evolutionary Conservation

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

See Also

References

  1. Deng Z, Roberts D, Wang X, Kemp RG. Expression, characterization, and crystallization of the pyrophosphate-dependent phosphofructo-1-kinase of Borrelia burgdorferi. Arch Biochem Biophys. 1999 Nov 15;371(2):326-31. PMID:10545221 doi:http://dx.doi.org/10.1006/abbi.1999.1446

1kzh, resolution 2.55Å

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