This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2coo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:27, 22 May 2024) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_2coo| PDB=2coo | SCENE= }}
 
-
===Solution structure of the e3_binding domain of dihydrolipoamide branched chaintransacylase===
 
-
==Disease==
+
==Solution structure of the e3_binding domain of dihydrolipoamide branched chaintransacylase==
-
[[http://www.uniprot.org/uniprot/ODB2_HUMAN ODB2_HUMAN]] Defects in DBT are the cause of maple syrup urine disease type 2 (MSUD2) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:1847055</ref><ref>PMID:9621512</ref>
+
<StructureSection load='2coo' size='340' side='right'caption='[[2coo]]' scene=''>
-
 
+
== Structural highlights ==
-
==Function==
+
<table><tr><td colspan='2'>[[2coo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2COO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2COO FirstGlance]. <br>
-
[[http://www.uniprot.org/uniprot/ODB2_HUMAN ODB2_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2coo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2coo OCA], [https://pdbe.org/2coo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2coo RCSB], [https://www.ebi.ac.uk/pdbsum/2coo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2coo ProSAT], [https://www.topsan.org/Proteins/RSGI/2coo TOPSAN]</span></td></tr>
-
==About this Structure==
+
</table>
-
[[2coo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2COO OCA].
+
== Disease ==
-
 
+
[https://www.uniprot.org/uniprot/ODB2_HUMAN ODB2_HUMAN] Defects in DBT are the cause of maple syrup urine disease type 2 (MSUD2) [MIM:[https://omim.org/entry/248600 248600]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:1847055</ref> <ref>PMID:9621512</ref>
-
==Reference==
+
== Function ==
-
<references group="xtra"/><references/>
+
[https://www.uniprot.org/uniprot/ODB2_HUMAN ODB2_HUMAN] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
 +
== 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/co/2coo_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=2coo ConSurf].
 +
<div style="clear:both"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Hayashi, F.]]
+
[[Category: Large Structures]]
-
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
+
[[Category: Hayashi F]]
-
[[Category: Yokoyama, S.]]
+
[[Category: Yokoyama S]]
-
[[Category: Zhang, H P.]]
+
[[Category: Zhang HP]]
-
[[Category: E3_binding domain]]
+
-
[[Category: Lipoamide acyltransferase component of branched-chain alpha-keto acid]]
+
-
[[Category: National project on protein structural and functional analyse]]
+
-
[[Category: Nppsfa]]
+
-
[[Category: Riken structural genomics/proteomics initiative]]
+
-
[[Category: Rsgi]]
+
-
[[Category: Structural genomic]]
+
-
[[Category: Transferase]]
+

Current revision

Solution structure of the e3_binding domain of dihydrolipoamide branched chaintransacylase

PDB ID 2coo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools