2qe7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_2qe7| PDB=2qe7 | SCENE= }}
+
==Crystal structure of the f1-atpase from the thermoalkaliphilic bacterium bacillus sp. ta2.a1==
-
===Crystal structure of the f1-atpase from the thermoalkaliphilic bacterium bacillus sp. ta2.a1===
+
<StructureSection load='2qe7' size='340' side='right' caption='[[2qe7]], [[Resolution|resolution]] 3.06&Aring;' scene=''>
-
{{ABSTRACT_PUBMED_17697996}}
+
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2qe7]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_sp._ta2.a1 Bacillus sp. ta2.a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QE7 FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jnv|1jnv]], [[1sky|1sky]]</td></tr>
 +
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">atpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90973 Bacillus sp. TA2.A1]), atpD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90973 Bacillus sp. TA2.A1]), atpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90973 Bacillus sp. TA2.A1]), atpC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90973 Bacillus sp. TA2.A1])</td></tr>
 +
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qe7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qe7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qe7 RCSB], [http://www.ebi.ac.uk/pdbsum/2qe7 PDBsum]</span></td></tr>
 +
<table>
 +
== 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/qe/2qe7_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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The ATP synthase of the thermoalkaliphilic Bacillus sp. TA2.A1 operates exclusively in ATP synthesis direction. In the crystal structure of the nucleotide-free alpha(3)beta(3)gamma epsilon subcomplex (TA2F(1)) at 3.1 A resolution, all three beta subunits adopt the open beta(E) conformation. The structure shows salt bridges between the helix-turn-helix motif of the C-terminal domain of the beta(E) subunit (residues Asp372 and Asp375) and the N-terminal helix of the gamma subunit (residues Arg9 and Arg10). These electrostatic forces pull the gamma shaft out of the rotational center and impede rotation through steric interference with the beta(E) subunit. Replacement of Arg9 and Arg10 with glutamines eliminates the salt bridges and results in an activation of ATP hydrolysis activity, suggesting that these salt bridges prevent the native enzyme from rotating in ATP hydrolysis direction. A similar bending of the gamma shaft as in the TA2F(1) structure was observed by single-particle analysis of the TA2F(1)F(o) holoenzyme.
-
==Function==
+
The structural basis for unidirectional rotation of thermoalkaliphilic F1-ATPase.,Stocker A, Keis S, Vonck J, Cook GM, Dimroth P Structure. 2007 Aug;15(8):904-14. PMID:17697996<ref>PMID:17697996</ref>
-
[[http://www.uniprot.org/uniprot/Q71CG2_9BACI Q71CG2_9BACI]] Produces ATP from ADP in the presence of a proton gradient across the membrane (By similarity).[HAMAP-Rule:MF_00530] [[http://www.uniprot.org/uniprot/Q71CG5_9BACI Q71CG5_9BACI]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit (By similarity).[HAMAP-Rule:MF_01346] [[http://www.uniprot.org/uniprot/Q71CG4_9BACI Q71CG4_9BACI]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex (By similarity).[HAMAP-Rule:MF_00815][RuleBase:RU004001][SAAS:SAAS023632_004_025650] [[http://www.uniprot.org/uniprot/Q71CG3_9BACI Q71CG3_9BACI]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits (By similarity).[HAMAP-Rule:MF_01347]
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[2qe7]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_sp._ta2.a1 Bacillus sp. ta2.a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QE7 OCA].
+
</div>
-
==Reference==
+
==See Also==
-
<ref group="xtra">PMID:017697996</ref><references group="xtra"/><references/>
+
*[[ATPase|ATPase]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Bacillus sp. ta2 a1]]
[[Category: Bacillus sp. ta2 a1]]
[[Category: Cook, G M.]]
[[Category: Cook, G M.]]

Revision as of 04:23, 3 October 2014

Crystal structure of the f1-atpase from the thermoalkaliphilic bacterium bacillus sp. ta2.a1

2qe7, resolution 3.06Å

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/2qe7"
Views
Personal tools
Navigation
Toolbox