4ald

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(Difference between revisions)

Revision as of 18:55, 9 February 2016

HUMAN MUSCLE FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COMPLEXED WITH FRUCTOSE 1,6-BISPHOSPHATE

Structural highlights

4ald is a 1 chain structure with sequence from Homo sapiens. 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.
Ligands:
Activity:	Fructose-bisphosphate aldolase, with EC number 4.1.2.13
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Disease

[ALDOA_HUMAN] Defects in ALDOA are the cause of glycogen storage disease type 12 (GSD12) [MIM:611881]; also known as red cell aldolase deficiency. A metabolic disorder associated with increased hepatic glycogen and hemolytic anemia. It may lead to myopathy with exercise intolerance and rhabdomyolysis.^[1] ^[2] ^[3] ^[4] ^[5]

Function

[ALDOA_HUMAN] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity).

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 catalyzes the reversible cleavage of fructose 1,6-bisphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde 3-phosphate or glyceraldehyde, respectively. Catalysis involves the formation of a Schiff's base intermediate formed at the epsilon-amino group of Lys229. The existing apo-enzyme structure was refined using the crystallographic free-R-factor and maximum likelihood methods that have been shown to give improved structural results that are less subject to model bias. Crystals were also soaked with the natural substrate (fructose 1,6-bisphosphate), and the crystal structure of this complex has been determined to 2.8 A. The apo structure differs from the previous Brookhaven-deposited structure (1ald) in the flexible C-terminal region. This is also the region where the native and complex structures exhibit differences. The conformational changes between native and complex structure are not large, but the observed complex does not involve the full formation of the Schiff's base intermediate, and suggests a preliminary hydrogen-bonded Michaelis complex before the formation of the covalent complex.

Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications.,Dalby A, Dauter Z, Littlechild JA Protein Sci. 1999 Feb;8(2):291-7. PMID:10048322^[6]

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

References

↑ Esposito G, Vitagliano L, Costanzo P, Borrelli L, Barone R, Pavone L, Izzo P, Zagari A, Salvatore F. Human aldolase A natural mutants: relationship between flexibility of the C-terminal region and enzyme function. Biochem J. 2004 May 15;380(Pt 1):51-6. PMID:14766013 doi:10.1042/BJ20031941
↑ Kishi H, Mukai T, Hirono A, Fujii H, Miwa S, Hori K. Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8623-7. PMID:2825199
↑ Takasaki Y, Takahashi I, Mukai T, Hori K. Human aldolase A of a hemolytic anemia patient with Asp-128----Gly substitution: characteristics of an enzyme generated in E. coli transfected with the expression plasmid pHAAD128G. J Biochem. 1990 Aug;108(2):153-7. PMID:2229018
↑ Kreuder J, Borkhardt A, Repp R, Pekrun A, Gottsche B, Gottschalk U, Reichmann H, Schachenmayr W, Schlegel K, Lampert F. Brief report: inherited metabolic myopathy and hemolysis due to a mutation in aldolase A. N Engl J Med. 1996 Apr 25;334(17):1100-4. PMID:8598869 doi:http://dx.doi.org/10.1056/NEJM199604253341705
↑ Yao DC, Tolan DR, Murray MF, Harris DJ, Darras BT, Geva A, Neufeld EJ. Hemolytic anemia and severe rhabdomyolysis caused by compound heterozygous mutations of the gene for erythrocyte/muscle isozyme of aldolase, ALDOA(Arg303X/Cys338Tyr). Blood. 2004 Mar 15;103(6):2401-3. Epub 2003 Nov 13. PMID:14615364 doi:10.1182/blood-2003-09-3160
↑ Dalby A, Dauter Z, Littlechild JA. Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications. Protein Sci. 1999 Feb;8(2):291-7. PMID:10048322

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ald"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2FP:1,6-FRUCTOSE+DIPHOSPHATE+(LINEAR+FORM)'>2FP</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ald FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ald OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ald RCSB], [http://www.ebi.ac.uk/pdbsum/4ald 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=4ald FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ald OCA], [http://pdbe.org/4ald PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ald RCSB], [http://www.ebi.ac.uk/pdbsum/4ald PDBsum]</span></td></tr>
 </table>
 == Disease ==
@@ Line 19: / Line 19: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=4ald ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ald" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Aldolase|Aldolase]]
+*[[Enzimas: complejo enzima-sustrato|Enzimas: complejo enzima-sustrato]]
+*[[Enzymes: enzyme-substrate complex|Enzymes: enzyme-substrate complex]]
+*[[Enzymes: enzyme-substrate complex (spanish)|Enzymes: enzyme-substrate complex (spanish)]]
 *[[Fructose Bisphosphate Aldolase|Fructose Bisphosphate Aldolase]]
 == References ==

4ald

From Proteopedia

Revision as of 18:55, 9 February 2016

HUMAN MUSCLE FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COMPLEXED WITH FRUCTOSE 1,6-BISPHOSPHATE

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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