3e4g

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of bovine coupling Factor B, G28E mutant

Structural highlights

3e4g is a 1 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 0.96Å
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/3e4g"

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

@@ Line 3: / Line 3: @@
 <StructureSection load='3e4g' size='340' side='right'caption='[[3e4g]], [[Resolution|resolution]] 0.96&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3e4g]] is a 1 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=3E4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E4G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3e4g]] is a 1 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=3E4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E4G 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>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 0.96&#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]], [[3e2j|3e2j]], [[3e3z|3e3z]]</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>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=3e4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4g OCA], [https://pdbe.org/3e4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e4g RCSB], [https://www.ebi.ac.uk/pdbsum/3e4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e4g 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]]

3e4g

From Proteopedia

Current revision

Crystal structure of bovine coupling Factor B, G28E mutant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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