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.

1ojx

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of an Archaeal fructose 1,6-bisphosphate aldolase

Structural highlights

1ojx is a 10 chain structure with sequence from Thermoproteus tenax. The February 2004 RCSB PDB Molecule of the Month feature on The Glycolytic Enzymes by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALF1_THETK Catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).

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-1,6-bisphosphate aldolase (FBPA) catalyzes the reversible cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate in the glycolytic pathway. FBPAs from archaeal organisms have recently been identified and characterized as a divergent family of proteins. Here, we report the first crystal structure of an archaeal FBPA at 1.9-A resolution. The structure of this 280-kDa protein complex was determined using single wavelength anomalous dispersion followed by 10-fold non-crystallographic symmetry averaging and refined to an R-factor of 14.9% (Rfree 17.9%). The protein forms a dimer of pentamers, consisting of subunits adopting the ubiquitous (betaalpha)8 barrel fold. Additionally, a crystal structure of the archaeal FBPA covalently bound to dihydroxyacetone phosphate was solved at 2.1-A resolution. Comparison of the active site residues with those of classical FBPAs, which share no significant sequence identity but display the same overall fold, reveals a common ancestry between these two families of FBPAs. Structural comparisons, furthermore, establish an evolutionary link to the triosephosphate isomerases, a superfamily hitherto considered independent from the superfamily of aldolases.

Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins.,Lorentzen E, Pohl E, Zwart P, Stark A, Russell RB, Knura T, Hensel R, Siebers B J Biol Chem. 2003 Nov 21;278(47):47253-60. Epub 2003 Aug 26. PMID:12941964^[1]

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

References

↑ Lorentzen E, Pohl E, Zwart P, Stark A, Russell RB, Knura T, Hensel R, Siebers B. Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins. J Biol Chem. 2003 Nov 21;278(47):47253-60. Epub 2003 Aug 26. PMID:12941964 doi:http://dx.doi.org/10.1074/jbc.M305922200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1ojx' size='340' side='right'caption='[[1ojx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ojx]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35583 Atcc 35583]. The February 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''The Glycolytic Enzymes''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_2 10.2210/rcsb_pdb/mom_2004_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OJX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ojx]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. The February 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''The Glycolytic Enzymes''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_2 10.2210/rcsb_pdb/mom_2004_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OJX FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ok4|1ok4]], [[1ok6|1ok6]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] </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=1ojx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ojx OCA], [https://pdbe.org/1ojx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ojx RCSB], [https://www.ebi.ac.uk/pdbsum/1ojx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ojx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ALF1_THETK ALF1_THETK]] Catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).
+[https://www.uniprot.org/uniprot/ALF1_THETK ALF1_THETK] Catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 35583]]
-[[Category: Fructose-bisphosphate aldolase]]
 [[Category: Large Structures]]
 [[Category: RCSB PDB Molecule of the Month]]
 [[Category: The Glycolytic Enzymes]]
-[[Category: Hensel, R]]
+[[Category: Thermoproteus tenax]]
-[[Category: Lorentzen, E]]
+[[Category: Hensel R]]
-[[Category: Pohl, E]]
+[[Category: Lorentzen E]]
-[[Category: Siebers, B]]
+[[Category: Pohl E]]
-[[Category: Stark, A]]
+[[Category: Siebers B]]
-[[Category: Zwart, P]]
+[[Category: Stark A]]
-[[Category: 6-bisphosphate]]
+[[Category: Zwart P]]
-[[Category: Aldolase]]
-[[Category: Archaeal]]
-[[Category: Fructose 1]]
-[[Category: Glycolytic]]
-[[Category: Lyase]]
-[[Category: Tim barrel]]

1ojx

From Proteopedia

Current revision

Crystal structure of an Archaeal fructose 1,6-bisphosphate aldolase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox