1aqt: Difference between revisions

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[[Image:1aqt.gif|left|200px]]


{{Structure
==EPSILON SUBUNIT OF F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI==
|PDB= 1aqt |SIZE=350|CAPTION= <scene name='initialview01'>1aqt</scene>, resolution 2.3&Aring;
<StructureSection load='1aqt' size='340' side='right'caption='[[1aqt]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1aqt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AQT FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aqt OCA], [https://pdbe.org/1aqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aqt RCSB], [https://www.ebi.ac.uk/pdbsum/1aqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aqt ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATPE_ECOLI ATPE_ECOLI] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530]
== 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/aq/1aqt_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=1aqt ConSurf].
<div style="clear:both"></div>


'''EPSILON SUBUNIT OF F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI'''
==See Also==
 
*[[ATPase 3D structures|ATPase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
BACKGROUND: Proton-translocating ATP synthases convert the energy generated from photosynthesis or respiration into ATP. These enzymes, termed F0F1-ATPases, are structurally highly conserved. In Escherichia coli, F0F1-ATPase consists of a membrane portion, F0, made up of three different polypeptides (a, b and c) and an F1 portion comprising five different polypeptides in the stoichiometry alpha 3 beta 3 gamma delta epsilon. The minor subunits gamma, delta and epsilon are required for the coupling of proton translocation with ATP synthesis; the epsilon subunit is in close contact with the alpha, beta, gamma and c subunits. The structure of the epsilon subunit provides clues to its essential role in this complex enzyme. RESULTS: The structure of the E. coli F0F1-ATPase epsilon subunit has been solved at 2.3 A resolution by multiple isomorphous replacement. The structure, comprising residues 2-136 of the polypeptide chain and 14 water molecules, refined to an R value of 0.214 (Rfree = 0.288). The molecule has a novel fold with two domains. The N-terminal domain is a beta sandwich with two five-stranded sheets. The C-terminal domain is formed from two alpha helices arranged in an antiparallel coiled-coil. A series of alanine residues from each helix form the central contacting residues in the helical domain and can be described as an 'alanine zipper'. There is an extensive hydrophobic contact region between the two domains providing a stable interface. The individual domains of the crystal structure closely resemble the structures determined in solution by NMR spectroscopy. CONCLUSIONS: Sequence alignments of a number of epsilon subunits from diverse sources suggest that the C-terminal domain, which is absent in some species, is not essential for function. In the crystal the N-terminal domains of two epsilon subunits make a close hydrophobic interaction across a crystallographic twofold axis. This region has previously been proposed as the contact surface between the epsilon and gamma subunits in the complete F1-ATPase complex. In the crystal structure we observe what is apparently a stable interface between the two domains of the epsilon subunit, consistent with the fact that the crystal and solution structures are quite similar despite close crystal packing. This suggests that a gross conformational change in the epsilon subunit, to transmit the effect of proton translocation to the catalytic domain, is unlikely, but cannot be ruled out.
 
==About this Structure==
1AQT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQT OCA].
 
==Reference==
Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli., Uhlin U, Cox GB, Guss JM, Structure. 1997 Sep 15;5(9):1219-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9331422 9331422]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: H(+)-transporting two-sector ATPase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Guss JM]]
[[Category: Guss, J M.]]
[[Category: Uhlin U]]
[[Category: Uhlin, U.]]
[[Category: atp synthase]]
[[Category: atpase]]
[[Category: epsilon subunit]]
[[Category: hydrolase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:01:08 2008''

Latest revision as of 09:32, 7 February 2024

EPSILON SUBUNIT OF F1F0-ATP SYNTHASE FROM ESCHERICHIA COLIEPSILON SUBUNIT OF F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI

Structural highlights

1aqt is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATPE_ECOLI Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1aqt, resolution 2.30Å

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