This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2vpw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2vpw" [edit=sysop:move=sysop])
Current revision (10:02, 9 May 2024) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2vpw.png|left|200px]]
 
-
{{STRUCTURE_2vpw| PDB=2vpw | SCENE= }}
+
==Polysulfide reductase with bound menaquinone==
 +
<StructureSection load='2vpw' size='340' side='right'caption='[[2vpw]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2vpw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VPW 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]] 3.1&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=MO:MOLYBDENUM+ATOM'>MO</scene>, <scene name='pdbligand=MQ7:MENAQUINONE-7'>MQ7</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=2vpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpw OCA], [https://pdbe.org/2vpw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vpw RCSB], [https://www.ebi.ac.uk/pdbsum/2vpw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vpw ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q72LA4_THET2 Q72LA4_THET2]
 +
== 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/vp/2vpw_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=2vpw ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Bacterial polysulfide reductase (PsrABC) is an integral membrane protein complex responsible for quinone-coupled reduction of polysulfide, a process important in extreme environments such as deep-sea vents and hot springs. We determined the structure of polysulfide reductase from Thermus thermophilus at 2.4-A resolution, revealing how the PsrA subunit recognizes and reduces its unique polyanionic substrate. The integral membrane subunit PsrC was characterized using the natural substrate menaquinone-7 and inhibitors, providing a comprehensive representation of a quinone binding site and revealing the presence of a water-filled cavity connecting the quinone binding site on the periplasmic side to the cytoplasm. These results suggest that polysulfide reductase could be a key energy-conserving enzyme of the T. thermophilus respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane via a previously unknown mechanism.
-
===POLYSULFIDE REDUCTASE WITH BOUND MENAQUINONE===
+
Molecular mechanism of energy conservation in polysulfide respiration.,Jormakka M, Yokoyama K, Yano T, Tamakoshi M, Akimoto S, Shimamura T, Curmi P, Iwata S Nat Struct Mol Biol. 2008 Jul;15(7):730-7. Epub 2008 Jun 8. PMID:18536726<ref>PMID:18536726</ref>
-
{{ABSTRACT_PUBMED_18536726}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 2vpw" style="background-color:#fffaf0;"></div>
-
[[2vpw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPW OCA].
+
== References ==
-
[[Category: Thermus thermophilus]]
+
<references/>
-
[[Category: Akimoto, S.]]
+
__TOC__
-
[[Category: Curmi, P.]]
+
</StructureSection>
-
[[Category: Iwata, S.]]
+
[[Category: Large Structures]]
-
[[Category: Jormakka, M.]]
+
[[Category: Thermus thermophilus HB27]]
-
[[Category: Shimamura, T.]]
+
[[Category: Akimoto S]]
-
[[Category: Tamakoshi, M.]]
+
[[Category: Curmi P]]
-
[[Category: Yano, T.]]
+
[[Category: Iwata S]]
-
[[Category: Yokoyama, K.]]
+
[[Category: Jormakka M]]
-
[[Category: Iron]]
+
[[Category: Shimamura T]]
-
[[Category: Iron-sulfur]]
+
[[Category: Tamakoshi M]]
-
[[Category: Membrane protein]]
+
[[Category: Yano T]]
-
[[Category: Metal-binding]]
+
[[Category: Yokoyama K]]
-
[[Category: Molybdenum]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: Respiratory enzyme]]
+

Current revision

Polysulfide reductase with bound menaquinone

PDB ID 2vpw

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/2vpw"
Personal tools