3u39: Difference between revisions

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<StructureSection load='3u39' size='340' side='right'caption='[[3u39]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
<StructureSection load='3u39' size='340' side='right'caption='[[3u39]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3u39]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U39 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3u39]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U39 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7921&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pfkA, pfk ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/6-phosphofructokinase 6-phosphofructokinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.11 2.7.1.11] </span></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=3u39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u39 OCA], [https://pdbe.org/3u39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u39 RCSB], [https://www.ebi.ac.uk/pdbsum/3u39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u39 ProSAT]</span></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=3u39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u39 OCA], [https://pdbe.org/3u39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u39 RCSB], [https://www.ebi.ac.uk/pdbsum/3u39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u39 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/PFKA_GEOSE PFKA_GEOSE] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_00339]<ref>PMID:8136379</ref>  
The crystal structure of the unliganded form of Bacillus stearothermophilus phosphofructokinase (BsPFK) was determined using molecular replacement to 2.8 A resolution (Protein Data Bank entry 3U39 ). The apo BsPFK structure serves as the basis for the interpretation of any structural changes seen in the binary or ternary complexes. When the apo BsPFK structure is compared with the previously published liganded structures of BsPFK, the structural impact that the binding of the ligands produces is revealed. This comparison shows that the apo form of BsPFK resembles the substrate-bound form of BsPFK, a finding that differs from previous predictions.
 
Structure of the apo form of Bacillus stearothermophilus phosphofructokinase.,Mosser R, Reddy MC, Bruning JB, Sacchettini JC, Reinhart GD Biochemistry. 2012 Jan 24;51(3):769-75. Epub 2012 Jan 11. PMID:22212099<ref>PMID:22212099</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3u39" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 6-phosphofructokinase]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Atcc 12980]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bruning, J B]]
[[Category: Bruning JB]]
[[Category: Mosser, R]]
[[Category: Mosser R]]
[[Category: Reddy, M C.M]]
[[Category: Reddy MCM]]
[[Category: Reinhart, G D]]
[[Category: Reinhart GD]]
[[Category: Sacchettini, J C]]
[[Category: Sacchettini JC]]
[[Category: Pfk]]
[[Category: Transferase]]

Latest revision as of 16:47, 14 March 2024

Crystal Structure of the apo Bacillus Stearothermophilus phosphofructokinaseCrystal Structure of the apo Bacillus Stearothermophilus phosphofructokinase

Structural highlights

3u39 is a 4 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7921Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PFKA_GEOSE Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_00339][1]

See Also

References

  1. ↑ Byrnes M, Zhu X, Younathan ES, Chang SH. Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme. Biochemistry. 1994 Mar 22;33(11):3424-31. doi: 10.1021/bi00177a036. PMID:8136379 doi:http://dx.doi.org/10.1021/bi00177a036

3u39, resolution 2.79Å

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