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.

5zqz

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 22:54, 10 April 2020

Structure of human mitochondrial trifunctional protein, tetramer

5zqz, resolution 4.20Å

Structural highlights

5zqz is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	HADHA, HADH (HUMAN), HADHB, MSTP029 (HUMAN)
Activity:	Acetyl-CoA C-acyltransferase, with EC number 2.3.1.16
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[ECHA_HUMAN] Mitochondrial trifunctional protein deficiency;Acute fatty liver of pregnancy;Long chain 3-hydroxyacyl-CoA dehydrogenase deficiency. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [ECHB_HUMAN] Mitochondrial trifunctional protein deficiency. The disease is caused by mutations affecting the gene represented in this entry.

Function

[ECHA_HUMAN] Bifunctional subunit.

Publication Abstract from PubMed

The mitochondrial trifunctional protein (TFP) catalyzes three reactions in the fatty acid beta-oxidation process. Mutations in the two TFP subunits cause mitochondrial trifunctional protein deficiency and acute fatty liver of pregnancy that can lead to death. Here we report a 4.2-A cryo-electron microscopy alpha2beta2 tetrameric structure of the human TFP. The tetramer has a V-shaped architecture that displays a distinct assembly compared with the bacterial TFPs. A concave surface of the TFP tetramer interacts with the detergent molecules in the structure, suggesting that this region is involved in associating with the membrane. Deletion of a helical hairpin in TFPbeta decreases its binding to the liposomes in vitro and reduces its membrane targeting in cells. Our results provide the structural basis for TFP function and have important implications for fatty acid oxidation related diseases.

Cryo-EM structure of human mitochondrial trifunctional protein.,Liang K, Li N, Wang X, Dai J, Liu P, Wang C, Chen XW, Gao N, Xiao J Proc Natl Acad Sci U S A. 2018 Jun 18. pii: 1801252115. doi:, 10.1073/pnas.1801252115. PMID:29915090^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Liang K, Li N, Wang X, Dai J, Liu P, Wang C, Chen XW, Gao N, Xiao J. Cryo-EM structure of human mitochondrial trifunctional protein. Proc Natl Acad Sci U S A. 2018 Jun 18. pii: 1801252115. doi:, 10.1073/pnas.1801252115. PMID:29915090 doi:http://dx.doi.org/10.1073/pnas.1801252115

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5zqz"

@@ Line 3: / Line 3: @@
 <SX load='5zqz' size='340' side='right' viewer='molstar' caption='[[5zqz]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5zqz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZQZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZQZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5zqz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZQZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZQZ FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HADHA, HADH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HADHB, MSTP029 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acyltransferase Acetyl-CoA C-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.16 2.3.1.16] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zqz OCA], [http://pdbe.org/5zqz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zqz RCSB], [http://www.ebi.ac.uk/pdbsum/5zqz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zqz ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zqz OCA], [http://pdbe.org/5zqz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zqz RCSB], [http://www.ebi.ac.uk/pdbsum/5zqz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zqz ProSAT]</span></td></tr>
 </table>
 == Disease ==

5zqz

From Proteopedia

Revision as of 22:54, 10 April 2020

Structure of human mitochondrial trifunctional protein, tetramer

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox