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1hf9

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C-Terminal Coiled-Coil Domain from Bovine IF1

Structural highlights

1hf9 is a 2 chain structure with sequence from Bos taurus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATIF1_BOVIN Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

Bovine IF(1) is a basic, 84 amino acid residue protein that inhibits the hydrolytic action of the F(1)F(0) ATP synthase in mitochondria under anaerobic conditions. Its oligomerization state is dependent on pH. At a pH value below 6.5 it forms an active dimer. At higher pH values, two dimers associate to form an inactive tetramer. Here, we present the solution structure of a C-terminal fragment of IF(1) (44-84) containing all five of the histidine residues present in the sequence. Most unusually, the molecule forms an anti-parallel coiled-coil in which three of the five histidine residues occupy key positions at the dimer interface.

Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.,Gordon-Smith DJ, Carbajo RJ, Yang JC, Videler H, Runswick MJ, Walker JE, Neuhaus D J Mol Biol. 2001 Apr 27;308(2):325-39. PMID:11327770^[7]

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

References

↑ Klein G, Satre M, Dianoux AC, Vignais PV. Radiolabeling of natural adenosine triphosphatase inhibitor with phenyl (14C)isothiocyanate and study of its interaction with mitochondrial adenosine triphosphatase. Localization of inhibitor binding sites and stoichiometry of binding. Biochemistry. 1980 Jun 24;19(13):2919-25. PMID:7397110
↑ Cabezon E, Butler PJ, Runswick MJ, Walker JE. Modulation of the oligomerization state of the bovine F1-ATPase inhibitor protein, IF1, by pH. J Biol Chem. 2000 Aug 18;275(33):25460-4. PMID:10831597 doi:10.1074/jbc.M003859200
↑ Ando C, Ichikawa N. Glutamic acid in the inhibitory site of mitochondrial ATPase inhibitor, IF(1), participates in pH sensing in both mammals and yeast. J Biochem. 2008 Oct;144(4):547-53. doi: 10.1093/jb/mvn100. Epub 2008 Aug 7. PMID:18687699 doi:http://dx.doi.org/10.1093/jb/mvn100
↑ Bason JV, Runswick MJ, Fearnley IM, Walker JE. Binding of the inhibitor protein IF(1) to bovine F(1)-ATPase. J Mol Biol. 2011 Feb 25;406(3):443-53. doi: 10.1016/j.jmb.2010.12.025. Epub 2010 , Dec 28. PMID:21192948 doi:http://dx.doi.org/10.1016/j.jmb.2010.12.025
↑ Cabezon E, Montgomery MG, Leslie AG, Walker JE. The structure of bovine F1-ATPase in complex with its regulatory protein IF1. Nat Struct Biol. 2003 Sep;10(9):744-50. Epub 2003 Aug 17. PMID:12923572 doi:http://dx.doi.org/10.1038/nsb966
↑ Gledhill JR, Montgomery MG, Leslie AG, Walker JE. How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria. Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15671-6. Epub 2007 Sep 25. PMID:17895376
↑ Gordon-Smith DJ, Carbajo RJ, Yang JC, Videler H, Runswick MJ, Walker JE, Neuhaus D. Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase. J Mol Biol. 2001 Apr 27;308(2):325-39. PMID:11327770 doi:http://dx.doi.org/10.1006/jmbi.2001.4570

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hf9"

@@ Line 1: / Line 1: @@
-[[Image:1hf9.png|left|200px]]
-{{STRUCTURE_1hf9|  PDB=1hf9  |  SCENE=  }}
+==C-Terminal Coiled-Coil Domain from Bovine IF1==
+<StructureSection load='1hf9' size='340' side='right'caption='[[1hf9]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1hf9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HF9 FirstGlance]. <br>
+</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=1hf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hf9 OCA], [https://pdbe.org/1hf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hf9 RCSB], [https://www.ebi.ac.uk/pdbsum/1hf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hf9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ATIF1_BOVIN ATIF1_BOVIN] Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase.<ref>PMID:7397110</ref> <ref>PMID:10831597</ref> <ref>PMID:18687699</ref> <ref>PMID:21192948</ref> <ref>PMID:12923572</ref> <ref>PMID:17895376</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bovine IF(1) is a basic, 84 amino acid residue protein that inhibits the hydrolytic action of the F(1)F(0) ATP synthase in mitochondria under anaerobic conditions. Its oligomerization state is dependent on pH. At a pH value below 6.5 it forms an active dimer. At higher pH values, two dimers associate to form an inactive tetramer. Here, we present the solution structure of a C-terminal fragment of IF(1) (44-84) containing all five of the histidine residues present in the sequence. Most unusually, the molecule forms an anti-parallel coiled-coil in which three of the five histidine residues occupy key positions at the dimer interface.
-===C-TERMINAL COILED-COIL DOMAIN FROM BOVINE IF1===
+Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.,Gordon-Smith DJ, Carbajo RJ, Yang JC, Videler H, Runswick MJ, Walker JE, Neuhaus D J Mol Biol. 2001 Apr 27;308(2):325-39. PMID:11327770<ref>PMID:11327770</ref>
-{{ABSTRACT_PUBMED_11327770}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1hf9" style="background-color:#fffaf0;"></div>
-[[1hf9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HF9 OCA].
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
-[[Category: Carbajo, R J.]]
+[[Category: Large Structures]]
-[[Category: Gordon-Smith, D J.]]
+[[Category: Carbajo RJ]]
-[[Category: Neuhaus, D.]]
+[[Category: Gordon-Smith DJ]]
-[[Category: Runswick, M J.]]
+[[Category: Neuhaus D]]
-[[Category: Videler, H.]]
+[[Category: Runswick MJ]]
-[[Category: Walker, J E.]]
+[[Category: Videler H]]
-[[Category: Yang, J C.]]
+[[Category: Walker JE]]
-[[Category: Atpase inhibitor]]
+[[Category: Yang J-C]]
-[[Category: F1 atpase inhibitor]]
-[[Category: Mitochondrion]]
-[[Category: Transit peptide]]

1hf9

From Proteopedia

Current revision

C-Terminal Coiled-Coil Domain from Bovine IF1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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