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3eiu

From Proteopedia

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{{Seed}}
 
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[[Image:3eiu.png|left|200px]]
 
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<!--
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==A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A1Ao ATP synthase==
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The line below this paragraph, containing "STRUCTURE_3eiu", creates the "Structure Box" on the page.
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<StructureSection load='3eiu' size='340' side='right'caption='[[3eiu]], [[Resolution|resolution]] 3.43&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3eiu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei Methanosarcina mazei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EIU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 3.43&#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=AES:4-(2-AMINOETHYL)BENZENESULFONYL+FLUORIDE'>AES</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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{{STRUCTURE_3eiu| PDB=3eiu | SCENE= }}
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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=3eiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eiu OCA], [https://pdbe.org/3eiu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eiu RCSB], [https://www.ebi.ac.uk/pdbsum/3eiu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eiu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VATB_METMA VATB_METMA] Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory 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/ei/3eiu_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=3eiu 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 adenosine triphosphate (ATP) entrance into the nucleotide-binding subunits of ATP synthases is a puzzle. In the previously determined structure of subunit B mutant R416W of the Methanosarcina mazei Go1 A-ATP synthase one ATP could be trapped at a transition position, close to the phosphate-binding loop. Using defined parameters for co-crystallization of an ATP-bound B-subunit, a unique transition position of ATP could be found in the crystallographic structure of this complex, solved at 3.4 A resolution. The nucleotide is found near the helix-turn-helix motif in the C-terminal domain of the protein; the location occupied by the gamma-subunit to interact with the empty beta-subunit in the thermoalkaliphilic Bacillus sp. TA2.A1 of the related F-ATP synthase. When compared with the determined structure of the ATP-transition position, close to the P-loop, and the nucleotide-free form of subunit B, the C-terminal domain of the B mutant is rotated by around 6 degrees, implicating an ATP moving pathway. We propose that, in the nucleotide empty state the central stalk subunit D is in close contact with subunit B and when the ATP molecule enters, D moves slightly, paving way for it to interact with the subunit B, which makes the C-terminal domain rotate by 6 degrees.
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===A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A1Ao ATP synthase===
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A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A(1)A(0) ATP synthase.,Manimekalai MS, Kumar A, Balakrishna AM, Gruber G J Struct Biol. 2009 Apr;166(1):38-45. Epub 2008 Dec 24. PMID:19138746<ref>PMID:19138746</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3eiu" style="background-color:#fffaf0;"></div>
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<!--
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19138746}}, adds the Publication Abstract to the page
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*[[ATPase 3D structures|ATPase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19138746 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19138746}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3EIU is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Methanosarcina_mazei Methanosarcina mazei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EIU OCA].
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==Reference==
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<ref group="xtra">PMID:19138746</ref><ref group="xtra">PMID:16563431</ref><references group="xtra"/>
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[[Category: Methanosarcina mazei]]
[[Category: Methanosarcina mazei]]
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[[Category: Balakrishna, A M.]]
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[[Category: Balakrishna AM]]
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[[Category: Gruber, G.]]
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[[Category: Gruber G]]
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[[Category: Kumar, A.]]
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[[Category: Kumar A]]
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[[Category: Manimekalai, S M.S.]]
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[[Category: Manimekalai SMS]]
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[[Category: Atp synthesis]]
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[[Category: Hydrogen ion transport]]
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[[Category: Hydrolase]]
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[[Category: Ion transport]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 16:04:40 2009''
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Current revision

A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A1Ao ATP synthase

PDB ID 3eiu

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