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==CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE== | |||
<StructureSection load='1f05' size='340' side='right'caption='[[1f05]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1f05]] is a 2 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=1F05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F05 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]] 2.45Å</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=1f05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f05 OCA], [https://pdbe.org/1f05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f05 RCSB], [https://www.ebi.ac.uk/pdbsum/1f05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f05 ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/TALDO_HUMAN TALDO_HUMAN] Defects in TALDO1 are the cause of transaldolase 1 deficiency (TALDO1 deficiency) [MIM:[https://omim.org/entry/606003 606003]. It results in telangiectases of the skin, hepatosplenomegaly, and enlarged clitoris. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TALDO_HUMAN TALDO_HUMAN] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | |||
== 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/f0/1f05_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=1f05 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of human transaldolase has been determined to 2.45 A resolution. The enzyme folds into an alpha/beta barrel structure and is thus similar in structure to other class I aldolases. Structure-based sequence alignment of available sequences of the transaldolase subfamily reveals that eight active site residues are invariant in the whole subfamily. Other invariant residues are mainly involved in the formation of the hydrophobic core of the enzyme. Noteworthy is a hydrophobic cluster consisting of five invariant residues. Human transaldolase has been implicated as an autoantigen in multiple sclerosis and four immunodominant peptide segments are located at the surface of the enzyme, accessible to autoantibodies. | |||
The three-dimensional structure of human transaldolase.,Thorell S, Gergely P Jr, Banki K, Perl A, Schneider G FEBS Lett. 2000 Jun 23;475(3):205-8. PMID:10869557<ref>PMID:10869557</ref> | |||
The | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1f05" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Transaldolase 3D structures|Transaldolase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Schneider G]] | |||
[[Category: Schneider | [[Category: Thorell S]] | ||
[[Category: Thorell | |||
Latest revision as of 09:01, 9 August 2023
CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASECRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE
Structural highlights
DiseaseTALDO_HUMAN Defects in TALDO1 are the cause of transaldolase 1 deficiency (TALDO1 deficiency) [MIM:606003. It results in telangiectases of the skin, hepatosplenomegaly, and enlarged clitoris. FunctionTALDO_HUMAN Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of human transaldolase has been determined to 2.45 A resolution. The enzyme folds into an alpha/beta barrel structure and is thus similar in structure to other class I aldolases. Structure-based sequence alignment of available sequences of the transaldolase subfamily reveals that eight active site residues are invariant in the whole subfamily. Other invariant residues are mainly involved in the formation of the hydrophobic core of the enzyme. Noteworthy is a hydrophobic cluster consisting of five invariant residues. Human transaldolase has been implicated as an autoantigen in multiple sclerosis and four immunodominant peptide segments are located at the surface of the enzyme, accessible to autoantibodies. The three-dimensional structure of human transaldolase.,Thorell S, Gergely P Jr, Banki K, Perl A, Schneider G FEBS Lett. 2000 Jun 23;475(3):205-8. PMID:10869557[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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