1ald

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<StructureSection load='1ald' size='340' side='right'caption='[[1ald]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1ald' size='340' side='right'caption='[[1ald]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ald]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ald]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALD FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=1ald FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ald OCA], [https://pdbe.org/1ald PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ald RCSB], [https://www.ebi.ac.uk/pdbsum/1ald PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ald ProSAT]</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=1ald FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ald OCA], [https://pdbe.org/1ald PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ald RCSB], [https://www.ebi.ac.uk/pdbsum/1ald PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ald ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/ALDOA_HUMAN ALDOA_HUMAN]] Defects in ALDOA are the cause of glycogen storage disease type 12 (GSD12) [MIM:[https://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>
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[https://www.uniprot.org/uniprot/ALDOA_HUMAN ALDOA_HUMAN] Defects in ALDOA are the cause of glycogen storage disease type 12 (GSD12) [MIM:[https://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 ==
== Function ==
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[[https://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).
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[https://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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1ald 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=1ald ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The structure of the type I fructose 1,6-bisphosphate aldolase from human muscle has been extended from 3 A to 2 A resolution. The improvement in the resulting electron density map is such that the 20 or so C-terminal residues, known to be associated with activity and isozyme specificity, have been located. The side-chain of the Schiff's base-forming lysine 229 is located towards the centre of an eight-stranded beta-barrel type structure. The C-terminal "tail" extends from the rim of the beta-barrel towards lysine 229, thus forming part of the active site of the enzyme. This structural arrangement appears to explain the difference in activity and specificity of the three tissue-specific human aldolases and helps with our understanding of the type I aldolase reaction mechanism.
 
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Activity and specificity of human aldolases.,Gamblin SJ, Davies GJ, Grimes JM, Jackson RM, Littlechild JA, Watson HC J Mol Biol. 1991 Jun 20;219(4):573-6. PMID:2056525<ref>PMID:2056525</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1ald" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fructose-bisphosphate aldolase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Watson, H C]]
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[[Category: Watson HC]]

Current revision

ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES

PDB ID 1ald

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