This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1l6w

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 21:17, 24 January 2018

Fructose-6-phosphate aldolase

Structural highlights

1l6w is a 10 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1onr, 1ucw, 1f05, 1i2o, 1i2p, 1i2q
Gene:	fsa ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FSAA_ECOLI] Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone (DHA) and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize several aldehydes as acceptor compounds in vitro, and hydroxyacetone (HA) or 1-hydroxy-butan-2-one as alternative donor substrate. Is also able to catalyze the direct stereoselective self-aldol addition of glycolaldehyde to furnish D-(-)-threose, and cross-aldol reactions of glycolaldehyde to other aldehyde acceptors. Is not able to cleave fructose, fructose 1-phosphate, glucose 6-phosphate, sedoheptulose 1,7-bisphosphate, xylulose 5-phosphate, ribulose 5-phosphate, and fructose 1,6-bisphosphate; cannot use dihydroxyacetone phosphate as donor compound nor D-glyceraldehyde as acceptor. Does not display transaldolase activity.^[1] [HAMAP-Rule:MF_00496]^[2] ^[3]

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 PubMed

Fructose-6-phosphate aldolase from Escherichia coli is a member of a small enzyme subfamily (MipB/TalC family) that belongs to the class I aldolases. The three-dimensional structure of this enzyme has been determined at 1.93 A resolution by single isomorphous replacement and tenfold non-crystallographic symmetry averaging and refined to an R-factor of 19.9% (R(free) 21.3%). The subunit folds into an alpha/beta barrel, with the catalytic lysine residue on barrel strand beta 4. It is very similar in overall structure to that of bacterial and mammalian transaldolases, although more compact due to extensive deletions of additional secondary structural elements. The enzyme forms a decamer of identical subunits with point group symmetry 52. Five subunits are arranged as a pentamer, and two ring-like pentamers pack like a doughnut to form the decamer. A major interaction within the pentamer is through the C-terminal helix from one monomer, which runs across the active site of the neighbouring subunit. In classical transaldolases, this helix folds back and covers the active site of the same subunit and is involved in dimer formation. The inter-subunit helix swapping appears to be a major determinant for the formation of pentamers rather than dimers while at the same time preserving importing interactions of this helix with the active site of the enzyme. The active site lysine residue is covalently modified, by forming a carbinolamine with glyceraldehyde from the crystallisation mixture. The catalytic machinery is very similar to that of transaldolase, which together with the overall structural similarity suggests that enzymes of the MipB/TALC subfamily are evolutionary related to the transaldolase family.

Crystal structure of decameric fructose-6-phosphate aldolase from Escherichia coli reveals inter-subunit helix swapping as a structural basis for assembly differences in the transaldolase family.,Thorell S, Schurmann M, Sprenger GA, Schneider G J Mol Biol. 2002 May 24;319(1):161-71. PMID:12051943^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schurmann M, Sprenger GA. Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases. J Biol Chem. 2001 Apr 6;276(14):11055-61. Epub 2000 Dec 18. PMID:11120740 doi:http://dx.doi.org/10.1074/jbc.M008061200
↑ Sugiyama M, Hong Z, Liang PH, Dean SM, Whalen LJ, Greenberg WA, Wong CH. D-Fructose-6-phosphate aldolase-catalyzed one-pot synthesis of iminocyclitols. J Am Chem Soc. 2007 Nov 28;129(47):14811-7. Epub 2007 Nov 7. PMID:17985886 doi:http://dx.doi.org/10.1021/ja073911i
↑ Garrabou X, Castillo JA, Guerard-Helaine C, Parella T, Joglar J, Lemaire M, Clapes P. Asymmetric self- and cross-aldol reactions of glycolaldehyde catalyzed by D-fructose-6-phosphate aldolase. Angew Chem Int Ed Engl. 2009;48(30):5521-5. doi: 10.1002/anie.200902065. PMID:19554584 doi:http://dx.doi.org/10.1002/anie.200902065
↑ Thorell S, Schurmann M, Sprenger GA, Schneider G. Crystal structure of decameric fructose-6-phosphate aldolase from Escherichia coli reveals inter-subunit helix swapping as a structural basis for assembly differences in the transaldolase family. J Mol Biol. 2002 May 24;319(1):161-71. PMID:12051943 doi:http://dx.doi.org/10.1016/S0022-2836(02)00258-9

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1l6w"

@@ Line 1: / Line 1: @@
 ==Fructose-6-phosphate aldolase==
 <StructureSection load='1l6w' size='340' side='right' caption='[[1l6w]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1onr|1onr]], [[1ucw|1ucw]], [[1f05|1f05]], [[1i2o|1i2o]], [[1i2p|1i2p]], [[1i2q|1i2q]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fsa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1l6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l6w OCA], [http://pdbe.org/1l6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l6w RCSB], [http://www.ebi.ac.uk/pdbsum/1l6w PDBsum]</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=1l6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l6w OCA], [http://pdbe.org/1l6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l6w RCSB], [http://www.ebi.ac.uk/pdbsum/1l6w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l6w ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l6/1l6w_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l6/1l6w_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1l6w" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Aldolase|Aldolase]]
 == References ==
 <references/>

1l6w

From Proteopedia

Revision as of 21:17, 24 January 2018

Fructose-6-phosphate aldolase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox