3mbd: Difference between revisions
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==Crystal structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi, bound to phosphate== | ==Crystal structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi, bound to phosphate== | ||
<StructureSection load='3mbd' size='340' side='right' caption='[[3mbd]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3mbd' size='340' side='right'caption='[[3mbd]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3mbd]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3mbd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Encephalitozoon_cuniculi Encephalitozoon cuniculi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MBD FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mbd OCA], [https://pdbe.org/3mbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mbd RCSB], [https://www.ebi.ac.uk/pdbsum/3mbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mbd ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ALF_ENCCU ALF_ENCCU] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Aldolase|Aldolase]] | *[[Aldolase 3D structures|Aldolase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Encephalitozoon cuniculi]] | ||
[[Category: | [[Category: Large Structures]] | ||
Latest revision as of 11:51, 6 September 2023
Crystal structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi, bound to phosphateCrystal structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi, bound to phosphate
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFructose bisphosphate aldolose (FBPA) enzymes have been found in a broad range of eukaryotic and prokaryotic organisms. FBPA catalyses the cleavage of fructose 1,6-bisphosphate into glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The SSGCID has reported several FBPA structures from pathogenic sources. Bioinformatic analysis of the genome of the eukaryotic microsporidian parasite Encephalitozoon cuniculi revealed an FBPA homolog. The structures of this enzyme in the presence of the native substrate FBP and also with the partial substrate analog phosphate are reported. The purified enzyme crystallized in 90 mM Bis-Tris propane pH 6.5, 18% PEG 3350, 18 mM NaKHPO(4), 10 mM urea for the phosphate-bound form and 100 mM Bis-Tris propane pH 6.5, 20% PEG 3350, 20 mM fructose 1,6-bisphosphate for the FBP-bound form. In both cases protein was present at 25 mg ml(-1) and the sitting-drop vapour-diffusion method was used. For the FBP-bound form, a data set to 2.37 A resolution was collected from a single crystal at 100 K. The crystal belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 121.46, b = 135.82, c = 61.54 A. The structure was refined to a final free R factor of 20.8%. For the phosphate-bound form, a data set was collected to 2.00 A resolution. The space group was also C222(1) and the unit-cell parameters were a = 121.96, b = 137.61, c = 62.23 A. The structure shares the typical barrel tertiary structure reported for previous FBPA structures and exhibits the same Schiff base in the active site. The quaternary structure is dimeric. This work provides a direct experimental result for the substrate-binding conformation of the product state of E. cuniculi FBPA. Structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi.,Gardberg A, Sankaran B, Davies D, Bhandari J, Staker B, Stewart L Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1055-9. Epub 2011 Aug 13. PMID:21904050[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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