5ey7: Difference between revisions
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<StructureSection load='5ey7' size='340' side='right' caption='[[5ey7]], [[Resolution|resolution]] 2.46Å' scene=''> | <StructureSection load='5ey7' size='340' side='right' caption='[[5ey7]], [[Resolution|resolution]] 2.46Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ey7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EY7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EY7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5ey7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibc3 Vibc3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EY7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EY7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eyn|5eyn]], [[5f0z|5f0z]], [[5f11|5f11]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eyn|5eyn]], [[5f0z|5f0z]], [[5f11|5f11]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cscK, VC0395_0600 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=345073 VIBC3])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructokinase Fructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.4 2.7.1.4] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructokinase Fructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.4 2.7.1.4] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ey7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ey7 OCA], [http://pdbe.org/5ey7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ey7 RCSB], [http://www.ebi.ac.uk/pdbsum/5ey7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ey7 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ey7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ey7 OCA], [http://pdbe.org/5ey7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ey7 RCSB], [http://www.ebi.ac.uk/pdbsum/5ey7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ey7 ProSAT]</span></td></tr> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Fructokinase]] | [[Category: Fructokinase]] | ||
[[Category: Vibc3]] | |||
[[Category: Nath, S]] | [[Category: Nath, S]] | ||
[[Category: Paul, R]] | [[Category: Paul, R]] | ||
Revision as of 04:13, 16 November 2017
Crystal structure of Fructokinase from Vibrio cholerae O395 in apo formCrystal structure of Fructokinase from Vibrio cholerae O395 in apo form
Structural highlights
Publication Abstract from PubMedFructokinase (FK), one of the crucial enzymes for sugar metabolism in bacterial systems, catalyses the unidirectional phosphorylation reaction from fructose to fructose 6-phosphate, thereby allowing parallel entry of fructose into glycolysis beside glucose. The cscK gene from Vibrio cholerae O395 coding for the enzyme FK has been cloned, overexpressed in Escherichia coli BL21 (DE3) and purified using Ni-NTA affinity chromatography. Crystals of V. cholerae FK (Vc-FK) and its cocrystal with fructose, adenosine diphosphate (ADP) and Mg2+ were grown in the presence of polyethylene glycol 6000 and diffracted to 2.45 and 1.75 A resolution, respectively. Analysis of the diffraction data showed that both crystal forms have symmetry consistent with space group P2(1)2(1)2, but with different unit-cell parameters. Assuming the presence of two molecules in the asymmetric unit, the Matthews coefficient for the apo Vc-FK crystals was estimated to be 2.4 A3 Da(-1), which corresponds to a solvent content of 48%. The corresponding values for the ADP- and sugar-bound Vc-FK crystals were 2.1 A3 Da(-1) and 40%, respectively, assuming the presence of one molecule in the asymmetric unit. Cloning, expression, purification, crystallization and preliminary X-ray analysis of a fructokinase from Vibrio cholerae O395.,Paul R, Nath S, Sen U Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1564-7., doi: 10.1107/S1744309112047598. Epub 2012 Nov 28. PMID:23192049[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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