1o97

From Proteopedia

(Difference between revisions)

Revision as of 10:07, 1 November 2017

Structure of electron transferring flavoprotein from Methylophilus methylotrophus, recognition loop removed by limited proteolysis

Structural highlights

1o97 is a 2 chain structure with sequence from Atcc 53528. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1e11, 1o94, 1o95, 1o96
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ETFB_METME] The electron transfer flavoprotein of this bacterium serves as an electron acceptor specifically for trimethylamine dehydrogenase. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). [ETFA_METME] The electron transfer flavoprotein of this bacterium serves as an electron acceptor specifically for trimethylamine dehydrogenase. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).

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

Here we report the crystal structures of a ternary electron transfer complex showing extensive motion at the protein interface. This physiological complex comprises the iron-sulfur flavoprotein trimethylamine dehydrogenase and electron transferring flavoprotein (ETF) from Methylophilus methylotrophus. In addition, we report the crystal structure of free ETF. In the complex, electron density for the FAD domain of ETF is absent, indicating high mobility. Positions for the FAD domain are revealed by molecular dynamics simulation, consistent with crystal structures and kinetic data. A dual interaction of ETF with trimethylamine dehydrogenase provides for dynamical motion at the protein interface: one site acts as an anchor, thereby allowing the other site to sample a large range of interactions, some compatible with rapid electron transfer. This study establishes the role of conformational sampling in multi-domain redox systems, providing insight into electron transfer between ETFs and structurally distinct redox partners.

Extensive conformational sampling in a ternary electron transfer complex.,Leys D, Basran J, Talfournier F, Sutcliffe MJ, Scrutton NS Nat Struct Biol. 2003 Mar;10(3):219-25. PMID:12567183^[1]

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

References

↑ Leys D, Basran J, Talfournier F, Sutcliffe MJ, Scrutton NS. Extensive conformational sampling in a ternary electron transfer complex. Nat Struct Biol. 2003 Mar;10(3):219-25. PMID:12567183 doi:http://dx.doi.org/10.1038/nsb894

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o97"

@@ Line 1: / Line 1: @@
-==STRUCTURE OF ELECTRON TRANSFERRING FLAVOPROTEIN FROM METHYLOPHILUS METHYLOTROPHUS, RECOGNITION LOOP REMOVED BY LIMITED PROTEOLYSIS==
+==Structure of electron transferring flavoprotein from Methylophilus methylotrophus, recognition loop removed by limited proteolysis==
 <StructureSection load='1o97' size='340' side='right' caption='[[1o97]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e11|1e11]], [[1o94|1o94]], [[1o95|1o95]], [[1o96|1o96]]</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=1o97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o97 OCA], [http://pdbe.org/1o97 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o97 RCSB], [http://www.ebi.ac.uk/pdbsum/1o97 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=1o97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o97 OCA], [http://pdbe.org/1o97 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o97 RCSB], [http://www.ebi.ac.uk/pdbsum/1o97 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o97 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1o97 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1o97

From Proteopedia

Revision as of 10:07, 1 November 2017

Structure of electron transferring flavoprotein from Methylophilus methylotrophus, recognition loop removed by limited proteolysis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox