1u7l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1u7l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u7l, resolution 1.75&Aring;" /> '''Crystal Structure of...)
Current revision (13:31, 13 March 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1u7l.jpg|left|200px]]<br /><applet load="1u7l" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1u7l, resolution 1.75&Aring;" />
 
-
'''Crystal Structure of subunit C (vma5p) of the yeast V-ATPase'''<br />
 
-
==Overview==
+
==Crystal Structure of subunit C (vma5p) of the yeast V-ATPase==
-
Vacuolar H(+)-ATPase (V-ATPase) has a crucial role in the vacuolar system, of eukaryotic cells. It provides most of the energy required for transport, systems that utilize the proton-motive force that is generated by ATP, hydrolysis. Some, but not all, of the V-ATPase subunits are homologous to, those of F-ATPase and the nonhomologous subunits determine the unique, features of V-ATPase. We determined the crystal structure of V-ATPase, subunit C (Vma5p), which does not show any homology with F-ATPase, subunits, at 1.75 A resolution. The structural features suggest that, subunit C functions as a flexible stator that holds together the catalytic, and membrane sectors of the enzyme. A second crystal form that was solved, at 2.9 A resolution supports the flexible nature of subunit C. These, structures provide a framework for exploring the unique mechanistic, features of V-ATPases.
+
<StructureSection load='1u7l' size='340' side='right'caption='[[1u7l]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1u7l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U7L 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]] 1.75&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=1u7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u7l OCA], [https://pdbe.org/1u7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u7l RCSB], [https://www.ebi.ac.uk/pdbsum/1u7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u7l ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/VATC_YEAST VATC_YEAST] Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C acts as a flexible stator that holds together the catalytic and the membrane sectors of the enzyme. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section. Binds ATP and is likely to have a specific function in the catalytic activity of the catalytic sector. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.<ref>PMID:10781598</ref>
 +
== 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/u7/1u7l_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=1u7l ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1U7L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with TLA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U7L OCA].
+
*[[ATPase 3D structures|ATPase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
Crystal structure of yeast V-ATPase subunit C reveals its stator function., Drory O, Frolow F, Nelson N, EMBO Rep. 2004 Dec;5(12):1148-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15540116 15540116]
+
__TOC__
-
[[Category: H(+)-transporting two-sector ATPase]]
+
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Single protein]]
+
[[Category: Drory O]]
-
[[Category: Drory, O.]]
+
[[Category: Frolow F]]
-
[[Category: Frolow, F.]]
+
[[Category: Nelson N]]
-
[[Category: Nelson, N.]]
+
-
[[Category: TLA]]
+
-
[[Category: hydrolase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:54:06 2007''
+

Current revision

Crystal Structure of subunit C (vma5p) of the yeast V-ATPase

PDB ID 1u7l

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/1u7l"
Personal tools