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3i4l

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{{STRUCTURE_3i4l| PDB=3i4l | SCENE= }}
 
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===Structural characterization for the nucleotide binding ability of subunit A with AMP-PNP of the A1AO ATP synthase===
 
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{{ABSTRACT_PUBMED_19944110}}
 
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==Function==
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==Structural characterization for the nucleotide binding ability of subunit A with AMP-PNP of the A1AO ATP synthase==
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[[http://www.uniprot.org/uniprot/VATA_PYRHO VATA_PYRHO]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
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<StructureSection load='3i4l' size='340' side='right'caption='[[3i4l]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3i4l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I4L FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i4l OCA], [https://pdbe.org/3i4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i4l RCSB], [https://www.ebi.ac.uk/pdbsum/3i4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i4l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VATA_PYRHO VATA_PYRHO] Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i4/3i4l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3i4l ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structures of the nucleotide-empty (A(E)), 5'-adenylyl-beta,gamma-imidodiphosphate (A(PNP))-bound, and ADP (A(DP))-bound forms of the catalytic A subunit of the energy producer A(1)A(O) ATP synthase from Pyrococcus horikoshii OT3 have been solved at 2.47 A and 2.4 A resolutions. The structures provide novel features of nucleotide binding and depict the residues involved in the catalysis of the A subunit. In the A(E) form, the phosphate analog SO(4)(2-) binds, via a water molecule, to the phosphate binding loop (P-loop) residue Ser238, which is also involved in the phosphate binding of ADP and 5'-adenylyl-beta,gamma-imidodiphosphate. Together with amino acids Gly234 and Phe236, the serine residue stabilizes the arched P-loop conformation of subunit A, as shown by the 2.4-A structure of the mutant protein S238A in which the P-loop flips into a relaxed state, comparable to the one in catalytic beta subunits of F(1)F(O) ATP synthases. Superposition of the existing P-loop structures of ATPases emphasizes the unique P-loop in subunit A, which is also discussed in the light of an evolutionary P-loop switch in related A(1)A(O) ATP synthases, F(1)F(O) ATP synthases, and vacuolar ATPases and implicates diverse catalytic mechanisms inside these biological motors.
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==About this Structure==
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Nucleotide binding states of subunit A of the A-ATP synthase and the implication of P-loop switch in evolution.,Kumar A, Manimekalai MS, Balakrishna AM, Jeyakanthan J, Gruber G J Mol Biol. 2010 Feb 19;396(2):301-20. Epub 2009 Nov 26. PMID:19944110<ref>PMID:19944110</ref>
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[[3i4l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrho Pyrho]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I4L OCA].
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==See Also==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[ATP synthase|ATP synthase]]
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</div>
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<div class="pdbe-citations 3i4l" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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<ref group="xtra">PMID:019944110</ref><references group="xtra"/><references/>
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*[[ATPase 3D structures|ATPase 3D structures]]
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[[Category: Pyrho]]
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== References ==
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[[Category: Balakrishna, A M.]]
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<references/>
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[[Category: Gruber, G.]]
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__TOC__
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[[Category: Jeyakanthan, J.]]
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</StructureSection>
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[[Category: Kumar, A.]]
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[[Category: Large Structures]]
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[[Category: Manimekalai, S M.S.]]
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[[Category: Pyrococcus horikoshii OT3]]
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[[Category: Hydrolase]]
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[[Category: Balakrishna AM]]
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[[Category: Gruber G]]
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[[Category: Jeyakanthan J]]
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[[Category: Kumar A]]
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[[Category: Manimekalai SMS]]

Current revision

Structural characterization for the nucleotide binding ability of subunit A with AMP-PNP of the A1AO ATP synthase

PDB ID 3i4l

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