5f3k: Difference between revisions

Revision as of 15:26, 2 March 2016

X-Ray Crystallographic Structure of hTrap1 N-terminal Domain-apo

Structural highlights

5f3k is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5f5r
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[TRAP1_HUMAN] Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, most likely through stabilization of mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA.^[1] ^[2] ^[3]

References

↑ Zhang L, Karsten P, Hamm S, Pogson JH, Muller-Rischart AK, Exner N, Haass C, Whitworth AJ, Winklhofer KF, Schulz JB, Voigt A. TRAP1 rescues PINK1 loss-of-function phenotypes. Hum Mol Genet. 2013 Jul 15;22(14):2829-41. doi: 10.1093/hmg/ddt132. Epub 2013 Mar, 21. PMID:23525905 doi:https://dx.doi.org/10.1093/hmg/ddt132
↑ Yoshida S, Tsutsumi S, Muhlebach G, Sourbier C, Lee MJ, Lee S, Vartholomaiou E, Tatokoro M, Beebe K, Miyajima N, Mohney RP, Chen Y, Hasumi H, Xu W, Fukushima H, Nakamura K, Koga F, Kihara K, Trepel J, Picard D, Neckers L. Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis. Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1604-12. doi:, 10.1073/pnas.1220659110. Epub 2013 Apr 5. PMID:23564345 doi:https://dx.doi.org/10.1073/pnas.1220659110
↑ Sciacovelli M, Guzzo G, Morello V, Frezza C, Zheng L, Nannini N, Calabrese F, Laudiero G, Esposito F, Landriscina M, Defilippi P, Bernardi P, Rasola A. The mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting succinate dehydrogenase. Cell Metab. 2013 Jun 4;17(6):988-99. doi: 10.1016/j.cmet.2013.04.019. PMID:23747254 doi:https://dx.doi.org/10.1016/j.cmet.2013.04.019

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OCA

[1] Zhang L, Karsten P, Hamm S, Pogson JH, Muller-Rischart AK, Exner N, Haass C, Whitworth AJ, Winklhofer KF, Schulz JB, Voigt A. TRAP1 rescues PINK1 loss-of-function phenotypes. Hum Mol Genet. 2013 Jul 15;22(14):2829-41. doi: 10.1093/hmg/ddt132. Epub 2013 Mar, 21. PMID:23525905 doi:https://dx.doi.org/10.1093/hmg/ddt132

[2] Yoshida S, Tsutsumi S, Muhlebach G, Sourbier C, Lee MJ, Lee S, Vartholomaiou E, Tatokoro M, Beebe K, Miyajima N, Mohney RP, Chen Y, Hasumi H, Xu W, Fukushima H, Nakamura K, Koga F, Kihara K, Trepel J, Picard D, Neckers L. Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis. Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1604-12. doi:, 10.1073/pnas.1220659110. Epub 2013 Apr 5. PMID:23564345 doi:https://dx.doi.org/10.1073/pnas.1220659110

[3] Sciacovelli M, Guzzo G, Morello V, Frezza C, Zheng L, Nannini N, Calabrese F, Laudiero G, Esposito F, Landriscina M, Defilippi P, Bernardi P, Rasola A. The mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting succinate dehydrogenase. Cell Metab. 2013 Jun 4;17(6):988-99. doi: 10.1016/j.cmet.2013.04.019. PMID:23747254 doi:https://dx.doi.org/10.1016/j.cmet.2013.04.019

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5f3k is ON HOLD  until Paper Publication
+==X-Ray Crystallographic Structure of hTrap1 N-terminal Domain-apo==
+<StructureSection load='5f3k' size='340' side='right' caption='[[5f3k]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
-Authors: Sung, N., Lee, J., Kim, J., Chang, C., Joachimiak, A., Lee, S., Tsai, F.T.F.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5f3k]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F3K FirstGlance]. <br>
-Description: X-Ray Crystallographic Structure of hTrap1 N-terminal Domain-apo
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f5r|5f5r]]</td></tr>
-[[Category: Unreleased Structures]]
+<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=5f3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f3k OCA], [http://pdbe.org/5f3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f3k RCSB], [http://www.ebi.ac.uk/pdbsum/5f3k PDBsum]</span></td></tr>
-[[Category: Sung, N]]
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TRAP1_HUMAN TRAP1_HUMAN]] Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, most likely through stabilization of mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA.<ref>PMID:23525905</ref> <ref>PMID:23564345</ref> <ref>PMID:23747254</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Chang, C]]
 [[Category: Joachimiak, A]]
+[[Category: Kim, J]]
 [[Category: Lee, J]]
 [[Category: Lee, S]]
-[[Category: Kim, J]]
+[[Category: Sung, N]]
-[[Category: Tsai, F.T.F]]
+[[Category: Tsai, F T.F]]
-[[Category: Chang, C]]
+[[Category: Apo]]
+[[Category: Chaperone]]
+[[Category: Hsp90]]
+[[Category: Trap1]]

5f3k: Difference between revisions

Revision as of 15:26, 2 March 2016

X-Ray Crystallographic Structure of hTrap1 N-terminal Domain-apo

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Function

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