5ky6
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Human muscle fructose-1,6-bisphosphate aldolase== | |
| + | <StructureSection load='5ky6' size='340' side='right' caption='[[5ky6]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ky6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KY6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ald|2ald]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALDOA, ALDA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ky6 OCA], [http://pdbe.org/5ky6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ky6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ky6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ky6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/ALDOA_HUMAN ALDOA_HUMAN]] Defects in ALDOA are the cause of glycogen storage disease type 12 (GSD12) [MIM:[http://omim.org/entry/611881 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.<ref>PMID:14766013</ref> <ref>PMID:2825199</ref> <ref>PMID:2229018</ref> <ref>PMID:8598869</ref> <ref>PMID:14615364</ref> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ALDOA_HUMAN ALDOA_HUMAN]] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:10048322</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5ky6" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Fructose-bisphosphate aldolase]] | ||
| + | [[Category: Human]] | ||
[[Category: Barciszewski, J]] | [[Category: Barciszewski, J]] | ||
| - | [[Category: Wisniewski, J]] | ||
[[Category: Jaskolski, M]] | [[Category: Jaskolski, M]] | ||
| + | [[Category: Rakus, D]] | ||
| + | [[Category: Wisniewski, J]] | ||
| + | [[Category: Aldolase]] | ||
| + | [[Category: Glycolysis]] | ||
| + | [[Category: Glyconeogenesis]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Muscle]] | ||
Revision as of 10:55, 6 November 2017
Human muscle fructose-1,6-bisphosphate aldolase
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