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.

2wp9

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:00, 4 November 2020

Crystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhB His207Thr mutant

Structural highlights

2wp9 is a 12 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , ,
Related:	2wdq, 2wdr, 1nen, 1nek, 2wu2, 2acz, 2wu5, 2wdv
Activity:	Succinate dehydrogenase (quinone), with EC number 1.3.5.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DHSD_ECOLI] Membrane-anchoring subunit of succinate dehydrogenase (SDH). [DHSA_ECOLI] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. [DHSC_ECOLI] Membrane-anchoring subunit of succinate dehydrogenase (SDH). [DHSB_ECOLI] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Succinate-ubiquinone oxidoreductase (SQR) and menaquinol-fumarate oxidoreductase (QFR) from Escherichia coli are members of the complex II family of enzymes. SQR and QFR catalyze similar reactions with quinones, however, SQR preferentially reacts with higher potential ubiquinones and QFR with lower potential napthoquinones. Both enzymes have a single functional quinone-binding site proximal to a [3Fe-4S] iron-sulfur cluster. A difference between SQR and QFR is that the redox potential of the [3Fe-4S] cluster in SQR is 140 mV higher than that found in QFR. This may reflect the character of the different quinones with which the two enzymes preferentially react. To investigate how the environment around the [3Fe-4S] cluster affects its redox properties and catalysis with quinones a conserved amino acid proximal to the cluster was mutated in both enzymes. It was found that substitution of SdhB His207 by threonine (like found in QFR) resulted in a 70 mV lowering of the redox potential of the cluster as measured by EPR. The converse mutation in QFR raised the redox potential of the cluster. X-ray structural analysis suggests that placing a charged residue near the [3Fe-4S] cluster is a primary reason for the alteration in redox potential with the hydrogen-bonding environment having a lesser effect. Steady state enzyme kinetic characterization of the mutant enzymes shows that the redox properties of the [3Fe-4S] cluster has only minor effect on catalysis.

Perturbation of the quinone binding site of complex II alters the electronic properties of the proximal [3Fe-4S] iron-sulfur cluster.,Ruprecht J, Iwata S, Rothery RA, Weiner JH, Maklashina E, Cecchini G J Biol Chem. 2011 Feb 10. PMID:21310949^[1]

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

References

↑ Ruprecht J, Iwata S, Rothery RA, Weiner JH, Maklashina E, Cecchini G. Perturbation of the quinone binding site of complex II alters the electronic properties of the proximal [3Fe-4S] iron-sulfur cluster. J Biol Chem. 2011 Feb 10. PMID:21310949 doi:10.1074/jbc.M110.209874

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wp9"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhB His207Thr mutant==
-<StructureSection load='2wp9' size='340' side='right' caption='[[2wp9]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='2wp9' size='340' side='right'caption='[[2wp9]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wp9]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WP9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WP9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wp9]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WP9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WP9 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBE:2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-CARBOXAMIDE'>CBE</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TEO:MALATE+LIKE+INTERMEDIATE'>TEO</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CBE:2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-CARBOXAMIDE'>CBE</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TEO:MALATE+LIKE+INTERMEDIATE'>TEO</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wdq|2wdq]], [[2wdr|2wdr]], [[1nen|1nen]], [[1nek|1nek]], [[2wu2|2wu2]], [[2acz|2acz]], [[2wu5|2wu5]], [[2wdv|2wdv]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase_(quinone) Succinate dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.1 1.3.5.1] </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=2wp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wp9 OCA], [http://pdbe.org/2wp9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wp9 RCSB], [http://www.ebi.ac.uk/pdbsum/2wp9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wp9 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wp9 OCA], [http://pdbe.org/2wp9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wp9 RCSB], [http://www.ebi.ac.uk/pdbsum/2wp9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wp9 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Succinate Dehydrogenase|Succinate Dehydrogenase]]
+*[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 38: @@
 </StructureSection>
 [[Category: Bacillus coli migula 1895]]
+[[Category: Large Structures]]
 [[Category: Cecchini, G]]
 [[Category: Iwata, S]]

2wp9

From Proteopedia

Revision as of 08:00, 4 November 2020

Crystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhB His207Thr mutant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox