1i2p: Difference between revisions
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<StructureSection load='1i2p' size='340' side='right'caption='[[1i2p]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='1i2p' size='340' side='right'caption='[[1i2p]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1i2p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1i2p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I2P 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]] 2.05Å</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=1i2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i2p OCA], [https://pdbe.org/1i2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i2p RCSB], [https://www.ebi.ac.uk/pdbsum/1i2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i2p 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=1i2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i2p OCA], [https://pdbe.org/1i2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i2p RCSB], [https://www.ebi.ac.uk/pdbsum/1i2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i2p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TALB_ECOLI TALB_ECOLI] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.[HAMAP-Rule:MF_00492] | |||
== 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== | ||
*[[Transaldolase|Transaldolase]] | *[[Transaldolase 3D structures|Transaldolase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jia J]] | |||
[[Category: Jia | [[Category: Schneider G]] | ||
[[Category: Schneider | [[Category: Thorell S]] | ||
[[Category: Thorell | |||
Latest revision as of 09:20, 9 August 2023
CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT D17ACRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT D17A
Structural highlights
FunctionTALB_ECOLI Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.[HAMAP-Rule:MF_00492] 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 PubMedThe roles of invariant residues at the active site of transaldolase B from Escherichia coli have been probed by site-directed mutagenesis. The mutant enzymes D17A, N35A, E96A, T156A, and S176A were purified from a talB-deficient host and analyzed with respect to their 3D structure and kinetic behavior. X-ray analysis showed that side chain replacement did not induce unanticipated structural changes in the mutant enzymes. Three mutations, N35A, E96A, and T156A resulted mainly in an effect on apparent kcat, with little changes in apparent Km values for the substrates. Residues N35 and T156 are involved in the positioning of a catalytic water molecule at the active site and the side chain of E96 participates in concert with this water molecule in proton transfer during catalysis. Substitution of Ser176 by alanine resulted in a mutant enzyme with 2.5% residual activity. The apparent Km value for the donor substrate, fructose 6-phosphate, was increased nearly fivefold while the apparent Km value for the acceptor substrate, erythrose 4-phosphate remained unchanged, consistent with a function for S176 in the binding of the C1 hydroxyl group of the donor substrate. The mutant D17A showed a 300-fold decrease in kcat, and a fivefold increase in the apparent Km value for the acceptor substrate erythrose 4-phosphate, suggesting a role of this residue in carbon-carbon bond cleavage and stabilization of the carbanion/enamine intermediate. Identification of catalytically important residues in the active site of Escherichia coli transaldolase.,Schorken U, Thorell S, Schurmann M, Jia J, Sprenger GA, Schneider G Eur J Biochem. 2001 Apr;268(8):2408-15. PMID:11298760[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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