2jtw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (19:05, 29 May 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2jtw.png|left|200px]]
 
-
<!--
+
==Solution structure of TM7 bound to DPC micelles==
-
The line below this paragraph, containing "STRUCTURE_2jtw", creates the "Structure Box" on the page.
+
<StructureSection load='2jtw' size='340' side='right'caption='[[2jtw]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2jtw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JTW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JTW FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2jtw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jtw OCA], [https://pdbe.org/2jtw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jtw RCSB], [https://www.ebi.ac.uk/pdbsum/2jtw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jtw ProSAT]</span></td></tr>
-
{{STRUCTURE_2jtw| PDB=2jtw | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/VPP1_YEAST VPP1_YEAST] Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:11278748, PubMed:1491220, PubMed:8798414). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:11278748, PubMed:1491220). Is present only in vacuolar V-ATPase complexes; enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion (PubMed:11278748, PubMed:8798414).<ref>PMID:11278748</ref> <ref>PMID:1491220</ref> <ref>PMID:8798414</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Many peptides, proteins, and drugs interact with biological membranes, and knowing the mode of binding is essential to understanding their biological functions. To obtain the complete orientation and immersion depth of such a compound, the membrane-mimetic system (micelle) is placed in an aqueous buffer containing the soluble and inert paramagnetic contrast agent Gd(DTPA-BMA). Paramagnetic relaxation enhancements (PREs) of a specific nucleus then depend only on its distance from the surface. The positioning of a structurally characterized compound can be obtained by least-squares fitting of experimental PREs to the micelle center position. This liquid-state NMR approach, which does not rely on isotopic labeling or chemical modification, has been applied to determine the location of the presumed transmembrane region 7 of yeast V-ATPase (TM7) and the membrane-bound antimicrobial peptide CM15 in micelles. TM7 binds in a trans-micelle orientation with the N-terminus being slightly closer to the surface than the C-terminus. CM15 is immersed unexpectedly deep into the micelle with the more hydrophilic side of the helix being closer to the surface than the hydrophobic one.
-
===Solution structure of TM7 bound to DPC micelles===
+
Positioning of Micelle-Bound Peptides by Paramagnetic Relaxation Enhancements.,Zangger K, Respondek M, Gobl C, Hohlweg W, Rasmussen K, Grampp G, Madl T J Phys Chem B. 2009 Mar 3. PMID:19256533<ref>PMID:19256533</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
==About this Structure==
+
</div>
-
2JTW is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JTW OCA].
+
<div class="pdbe-citations 2jtw" style="background-color:#fffaf0;"></div>
-
[[Category: Madl, T.]]
+
== References ==
-
[[Category: Respondek, M.]]
+
<references/>
-
[[Category: Zangger, K.]]
+
__TOC__
-
[[Category: Membrane protein]]
+
</StructureSection>
-
[[Category: Micelle-bound]]
+
[[Category: Large Structures]]
-
[[Category: Peptide]]
+
[[Category: Saccharomyces cerevisiae S288C]]
-
[[Category: Transmembrane]]
+
[[Category: Madl T]]
-
 
+
[[Category: Respondek M]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 18 20:06:07 2009''
+
[[Category: Zangger K]]

Current revision

Solution structure of TM7 bound to DPC micelles

PDB ID 2jtw

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools