4xa7

From Proteopedia

(Difference between revisions)

Revision as of 00:13, 26 January 2017

Soluble part of holo NqrC from V. harveyi

Structural highlights

4xa7 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[M7R347_VIBHA] NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.[HAMAP-Rule:MF_00427]

Publication Abstract from PubMed

Na+-translocating NADH:quinone oxidoreductase (NQR) is a redox-driven sodium pump operating in the respiratory chain of various bacteria, including pathogenic species. The enzyme has a unique set of redox active prosthetic groups, which includes two covalently bound flavin mononucleotide (FMN) residues attached to threonine residues in subunits NqrB and NqrC. The reason of FMN covalent bonding in the subunits has not been established yet. In the current work, binding of free FMN to the apo-form of NqrC from Vibrio harveyi was studied showing very low affinity of NqrC to FMN in the absence of its covalent bonding. To study structural aspects of flavin binding in NqrC, its holo-form was crystallized and its 3D structure was solved at 1.56 A resolution. It was found that the isoalloxazine moiety of the FMN residue is buried in a hydrophobic cavity and that its pyrimidine ring is squeezed between hydrophobic amino acid residues while its benzene ring is extended from the protein surroundings. This structure of the flavin-binding pocket appears to provide flexibility of the benzene ring, which can help the FMN residue to take the bended conformation and thus to stabilize the one-electron reduced form of the prosthetic group. These properties may also lead to relatively weak noncovalent binding of the flavin. This fact along with periplasmic location of the FMN-binding domains in the vast majority of NqrC-like proteins may explain the necessity of the covalent bonding of this prosthetic group to prevent its loss to the external medium.

Structural and Functional Investigation of Flavin Binding Center of the NqrC Subunit of Sodium-Translocating NADH:Quinone Oxidoreductase from Vibrio harveyi.,Borshchevskiy V, Round E, Bertsova Y, Polovinkin V, Gushchin I, Ishchenko A, Kovalev K, Mishin A, Kachalova G, Popov A, Bogachev A, Gordeliy V PLoS One. 2015 Mar 3;10(3):e0118548. doi: 10.1371/journal.pone.0118548., eCollection 2015. PMID:25734798^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Borshchevskiy V, Round E, Bertsova Y, Polovinkin V, Gushchin I, Ishchenko A, Kovalev K, Mishin A, Kachalova G, Popov A, Bogachev A, Gordeliy V. Structural and Functional Investigation of Flavin Binding Center of the NqrC Subunit of Sodium-Translocating NADH:Quinone Oxidoreductase from Vibrio harveyi. PLoS One. 2015 Mar 3;10(3):e0118548. doi: 10.1371/journal.pone.0118548., eCollection 2015. PMID:25734798 doi:http://dx.doi.org/10.1371/journal.pone.0118548

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4xa7"

@@ Line 1: / Line 1: @@
 ==Soluble part of holo NqrC from V. harveyi==
 <StructureSection load='4xa7' size='340' side='right' caption='[[4xa7]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4xa7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XA7 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xa7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xa7 RCSB], [http://www.ebi.ac.uk/pdbsum/4xa7 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xa7 OCA], [http://pdbe.org/4xa7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xa7 RCSB], [http://www.ebi.ac.uk/pdbsum/4xa7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xa7 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4xa7" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4xa7

From Proteopedia

Revision as of 00:13, 26 January 2017

Soluble part of holo NqrC from V. harveyi

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox