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
(New page: 200px<br /><applet load="1l6w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l6w, resolution 1.93&Aring;" /> '''Fructose-6-phosphate...)
Current revision (08:06, 3 April 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1l6w.gif|left|200px]]<br /><applet load="1l6w" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1l6w, resolution 1.93&Aring;" />
 
-
'''Fructose-6-phosphate aldolase'''<br />
 
-
==Overview==
+
==Fructose-6-phosphate aldolase==
-
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.
+
<StructureSection load='1l6w' size='340' side='right'caption='[[1l6w]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1l6w]] is a 10 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=1L6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L6W FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=1l6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l6w OCA], [https://pdbe.org/1l6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l6w RCSB], [https://www.ebi.ac.uk/pdbsum/1l6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l6w ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FSAA_ECOLI 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.<ref>PMID:11120740</ref> [HAMAP-Rule:MF_00496]<ref>PMID:17985886</ref> <ref>PMID:19554584</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<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>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l6w ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1L6W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L6W OCA].
+
*[[Aldolase 3D structures|Aldolase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12051943 12051943]
+
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Schneider, G.]]
+
[[Category: Schneider G]]
-
[[Category: Schuermann, M.]]
+
[[Category: Schuermann M]]
-
[[Category: Sprenger, G.A.]]
+
[[Category: Sprenger GA]]
-
[[Category: Thorell, S.]]
+
[[Category: Thorell S]]
-
[[Category: GOL]]
+
-
[[Category: alpha-beta barrel]]
+
-
[[Category: domain swapping]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:19:40 2007''
+

Current revision

Fructose-6-phosphate aldolase

PDB ID 1l6w

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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