1ald

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_1ald| PDB=1ald | SCENE= }}
+
==ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES==
-
===ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES===
+
<StructureSection load='1ald' size='340' side='right' caption='[[1ald]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
{{ABSTRACT_PUBMED_2056525}}
+
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1ald]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ALD FirstGlance]. <br>
 +
</td></tr><tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ald FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ald OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ald RCSB], [http://www.ebi.ac.uk/pdbsum/1ald PDBsum]</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).
 +
== 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/1ald_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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
==Disease==
+
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>
-
[[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==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[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>
-
 
+
-
==About this Structure==
+
-
[[1ald]] is a 1 chain structure with sequence from [http://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].
+
==See Also==
==See Also==
*[[Aldolase|Aldolase]]
*[[Aldolase|Aldolase]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:002056525</ref><references group="xtra"/><references/>
+
__TOC__
 +
</StructureSection>
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Watson, H C.]]
[[Category: Watson, H C.]]

Revision as of 14:12, 29 September 2014

ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES

1ald, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ald"
Views
Personal tools
Navigation
Toolbox