2ald: Difference between revisions

Latest revision as of 09:13, 14 February 2024

HUMAN MUSCLE ALDOLASE

Structural highlights

2ald is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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:https://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

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OCA

[1] 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

[2] 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

[3] 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

[4] 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:https://dx.doi.org/10.1056/NEJM199604253341705

[5] 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

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[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
-[[Image:2ald.gif|left|200px]]<br />
-<applet load="2ald" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2ald, resolution 2.1&Aring;" />
-'''HUMAN MUSCLE ALDOLASE'''<br />
-==Overview==
+==HUMAN MUSCLE ALDOLASE==
-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.
+<StructureSection load='2ald' size='340' side='right'caption='[[2ald]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+</table>
+== Disease ==
+[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 ==
+[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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/al/2ald_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <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/main_output.php?pdb_ID=2ald ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-ALD 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] Structure known Active Site: SBL. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ALD OCA].
+*[[Aldolase 3D structures|Aldolase 3D structures]]
+== References ==
-==Reference==
+<references/>
-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]
+__TOC__
-[[Category: Fructose-bisphosphate aldolase]]
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Dalby, A.R.]]
+[[Category: Dalby AR]]
-[[Category: Littlechild, J.A.]]
+[[Category: Littlechild JA]]
-[[Category: lyase (aldehyde)]]
-[[Category: type i aldolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 17:35:18 2007''

2ald: Difference between revisions

Latest revision as of 09:13, 14 February 2024

HUMAN MUSCLE ALDOLASE

Structural highlights

Disease

Function

Evolutionary Conservation

See Also

References

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