3e2j

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of bovine coupling factor B

Structural highlights

3e2j is a 4 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATP5S_BOVIN Involved in regulation of mitochondrial membrane ATP synthase. Necessary for H(+) conduction of ATP synthase. Facilitates energy-driven catalysis of ATP synthesis by blocking a proton leak through an alternative proton exit pathway.^[1] ^[2]

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 PubMed

Coupling factor B (FB) is a mitochondrial inner membrane polypeptide that facilitates the energy-driven catalysis of ATP synthesis in animal mitochondria by blocking a proton leak across the membrane. Here, we report the crystal structure of the bovine mitochondrial FB mutant with Gly-3-Glu substitution determined at a resolution of 0.96 A and that of the WT polypeptide at a resolution of 2.9 A. The structure reveals an oblong, oval-shaped molecule with a unique globular N-terminal domain that is proposed to be the membrane anchor domain and the capping region to the C-terminal leucine-rich repeats domain. A short N-terminal alpha-helix, which extends away from the molecule's body, is suggestive of functioning as an anchor for FB to the matrix side of the mitochondrial inner membrane. Identification of a bound Mg(2+) ion reveals that FB is a metalloprotein. We also report the cocrystal structures of FB bound with phenylarsine oxide and Cd(2+), two known inhibitors of the FB coupling activity.

Crystal structure of bovine mitochondrial factor B at 0.96-A resolution.,Lee JK, Belogrudov GI, Stroud RM Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13379-84. Epub 2008 Sep 3. PMID:18768789^[3]

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

References

↑ Belogrudov GI. Factor B is essential for ATP synthesis by mitochondria. Arch Biochem Biophys. 2002 Oct 15;406(2):271-4. PMID:12361715
↑ Lee JK, Belogrudov GI, Stroud RM. Crystal structure of bovine mitochondrial factor B at 0.96-A resolution. Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13379-84. Epub 2008 Sep 3. PMID:18768789
↑ Lee JK, Belogrudov GI, Stroud RM. Crystal structure of bovine mitochondrial factor B at 0.96-A resolution. Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13379-84. Epub 2008 Sep 3. PMID:18768789

1 Structural highlights
2 Function
3 Evolutionary Conservation
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/3e2j"

Categories: Bos taurus | Large Structures | Belogrudov GI | Lee JK | Stroud RM

@@ Line 3: / Line 3: @@
 <StructureSection load='3e2j' size='340' side='right'caption='[[3e2j]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3e2j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E2J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3e2j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E2J FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dze|3dze]], [[3e3z|3e3z]], [[3e4g|3e4g]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATP5S, ATPW ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></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=3e2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e2j OCA], [https://pdbe.org/3e2j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e2j RCSB], [https://www.ebi.ac.uk/pdbsum/3e2j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e2j ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ATP5S_BOVIN ATP5S_BOVIN]] Involved in regulation of mitochondrial membrane ATP synthase. Necessary for H(+) conduction of ATP synthase. Facilitates energy-driven catalysis of ATP synthesis by blocking a proton leak through an alternative proton exit pathway.<ref>PMID:12361715</ref> <ref>PMID:18768789</ref>
+[https://www.uniprot.org/uniprot/ATP5S_BOVIN ATP5S_BOVIN] Involved in regulation of mitochondrial membrane ATP synthase. Necessary for H(+) conduction of ATP synthase. Facilitates energy-driven catalysis of ATP synthesis by blocking a proton leak through an alternative proton exit pathway.<ref>PMID:12361715</ref> <ref>PMID:18768789</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bovin]]
+[[Category: Bos taurus]]
 [[Category: Large Structures]]
-[[Category: Belogrudov, G I]]
+[[Category: Belogrudov GI]]
-[[Category: Lee, J K]]
+[[Category: Lee JK]]
-[[Category: Stroud, R M]]
+[[Category: Stroud RM]]
-[[Category: Cf0]]
-[[Category: Electron transport]]
-[[Category: Hydrogen ion transport]]
-[[Category: Inner membrane]]
-[[Category: Ion transport]]
-[[Category: Leucine-rich repeat]]
-[[Category: Membrane]]
-[[Category: Mitochondrion]]
-[[Category: Transit peptide]]
-[[Category: Transport]]

3e2j

From Proteopedia

Current revision

Crystal structure of bovine coupling factor B

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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