1h8h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:20, 13 December 2023) (edit) (undo)
 
(20 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1h8h.jpg|left|200px]]<br /><applet load="1h8h" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1h8h, resolution 2.9&Aring;" />
 
-
'''BOVINE MITOCHONDRIAL F1-ATPASE CRYSTALLISED IN THE PRESENCE OF 5MM AMPPNP'''<br />
 
-
==Overview==
+
==Bovine mitochondrial F1-ATPase crystallised in the presence of 5mm AMPPNP==
-
Analysis of tryptophan mutants of F(1)-ATPase from Escherichia coli [Lobau, et al. (1997) FEBS Lett. 404, 15-18] suggested that nucleotide, concentrations used to grow crystals for the determination of the, structure of bovine F(1)-ATPase [Abrahams et al. (1994) Nature 370, 621-628] would be sufficient to occupy only two catalytic sites, and that, higher concentrations of nucleotide would result in all three sites being, occupied. We have determined the structure of bovine F(1)-ATPase at 2.9 A, resolution with crystals grown in the presence of 5 mM AMPPNP and 5 microM, ADP. Similar to previous structures of bovine F(1)-ATPase determined with, crystals grown in the presence of lower nucleotide concentrations, only, two beta-subunits have bound nucleotide and the third subunit remains, empty.
+
<StructureSection load='1h8h' size='340' side='right'caption='[[1h8h]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1h8h]] is a 7 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=1H8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H8H FirstGlance]. <br>
 +
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1h8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8h OCA], [https://pdbe.org/1h8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h8h RCSB], [https://www.ebi.ac.uk/pdbsum/1h8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h8h ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h8/1h8h_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h8h ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Analysis of tryptophan mutants of F(1)-ATPase from Escherichia coli [Lobau et al. (1997) FEBS Lett. 404, 15-18] suggested that nucleotide concentrations used to grow crystals for the determination of the structure of bovine F(1)-ATPase [Abrahams et al. (1994) Nature 370, 621-628] would be sufficient to occupy only two catalytic sites, and that higher concentrations of nucleotide would result in all three sites being occupied. We have determined the structure of bovine F(1)-ATPase at 2.9 A resolution with crystals grown in the presence of 5 mM AMPPNP and 5 microM ADP. Similar to previous structures of bovine F(1)-ATPase determined with crystals grown in the presence of lower nucleotide concentrations, only two beta-subunits have bound nucleotide and the third subunit remains empty.
-
==About this Structure==
+
The structure and nucleotide occupancy of bovine mitochondrial F(1)-ATPase are not influenced by crystallisation at high concentrations of nucleotide.,Menz RI, Leslie AG, Walker JE FEBS Lett. 2001 Apr 6;494(1-2):11-4. PMID:11297725<ref>PMID:11297725</ref>
-
1H8H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=ATP:'>ATP</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.3.14 Transferred entry: 3.6.3.14], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34] Known structural/functional Sites: <scene name='pdbsite=AC1:Atp+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Atp+Binding+Site+For+Chain+B'>AC3</scene>, <scene name='pdbsite=AC4:Mg+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Atp+Binding+Site+For+Chain+C'>AC5</scene>, <scene name='pdbsite=AC6:Mg+Binding+Site+For+Chain+C'>AC6</scene>, <scene name='pdbsite=AC7:Adp+Binding+Site+For+Chain+D'>AC7</scene>, <scene name='pdbsite=AC8:Mg+Binding+Site+For+Chain+D'>AC8</scene>, <scene name='pdbsite=AC9:Po4+Binding+Site+For+Chain+E'>AC9</scene>, <scene name='pdbsite=BC1:Atp+Binding+Site+For+Chain+F'>BC1</scene>, <scene name='pdbsite=BC2:Mg+Binding+Site+For+Chain+F'>BC2</scene>, <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+Glutamic+Aci+Residue+Is+Believe+...'>CAT</scene> and <scene name='pdbsite=PLP:LYS+Within+The+P-Loop+(Phosphate+Binding)+Motif,+Gxxxxgkt/S'>PLP</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8H OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
The structure and nucleotide occupancy of bovine mitochondrial F(1)-ATPase are not influenced by crystallisation at high concentrations of nucleotide., Menz RI, Leslie AG, Walker JE, FEBS Lett. 2001 Apr 6;494(1-2):11-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11297725 11297725]
+
</div>
-
[[Category: Bos taurus]]
+
<div class="pdbe-citations 1h8h" style="background-color:#fffaf0;"></div>
-
[[Category: Protein complex]]
+
-
[[Category: Transferred entry: 3.6.3.14]]
+
-
[[Category: Leslie, A.G.W.]]
+
-
[[Category: Menz, R.I.]]
+
-
[[Category: Walker, J.E.]]
+
-
[[Category: ADP]]
+
-
[[Category: ATP]]
+
-
[[Category: GOL]]
+
-
[[Category: MG]]
+
-
[[Category: PO4]]
+
-
[[Category: atp phosphorylase]]
+
-
[[Category: atp phosphorylase (h+ transporting)]]
+
-
[[Category: atp synthase]]
+
-
[[Category: f1-atpase]]
+
-
[[Category: f1fo atp synthase]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:47:42 2008''
+
==See Also==
 +
*[[ATPase 3D structures|ATPase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Bos taurus]]
 +
[[Category: Large Structures]]
 +
[[Category: Braig K]]
 +
[[Category: Leslie AGW]]
 +
[[Category: Menz RI]]
 +
[[Category: Montgomery MG]]
 +
[[Category: Walker JE]]

Current revision

Bovine mitochondrial F1-ATPase crystallised in the presence of 5mm AMPPNP

PDB ID 1h8h

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h8h"
Personal tools