2ald

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[[Image:2ald.jpg|left|200px]]<br /><applet load="2ald" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ald, resolution 2.1&Aring;" />
 
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'''HUMAN MUSCLE ALDOLASE'''<br />
 
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==Overview==
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==HUMAN MUSCLE ALDOLASE==
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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.
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<StructureSection load='2ald' size='340' side='right'caption='[[2ald]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ald]] 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=2ALD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ALD FirstGlance]. <br>
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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]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ald FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ald OCA], [https://pdbe.org/2ald PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ald RCSB], [https://www.ebi.ac.uk/pdbsum/2ald PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ald ProSAT]</span></td></tr>
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</table>
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== 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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== 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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/al/2ald_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2ald ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known disease associated with this structure: Aldolase A deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103850 103850]]
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2ALD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Known structural/functional Site: <scene name='pdbsite=SBL:Schiff'S+Base+LYS'>SBL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ALD OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10048322 10048322]
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[[Category: Fructose-bisphosphate aldolase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dalby, A.R.]]
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[[Category: Dalby AR]]
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[[Category: Littlechild, J.A.]]
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[[Category: Littlechild JA]]
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[[Category: lyase (aldehyde)]]
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[[Category: type i aldolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:22:58 2008''
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Current revision

HUMAN MUSCLE ALDOLASE

PDB ID 2ald

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