|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='2bmv' size='340' side='right'caption='[[2bmv]], [[Resolution|resolution]] 2.11Å' scene=''> | | <StructureSection load='2bmv' size='340' side='right'caption='[[2bmv]], [[Resolution|resolution]] 2.11Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bmv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BMV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2BMV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2bmv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BMV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11Å</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=2bmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmv OCA], [http://pdbe.org/2bmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bmv RCSB], [http://www.ebi.ac.uk/pdbsum/2bmv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bmv ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=2bmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmv OCA], [https://pdbe.org/2bmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bmv RCSB], [https://www.ebi.ac.uk/pdbsum/2bmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bmv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FLAV_HELPY FLAV_HELPY]] Low-potential electron donor to a number of redox enzymes (By similarity). | + | [https://www.uniprot.org/uniprot/FLAV_HELPY FLAV_HELPY] Low-potential electron donor to a number of redox enzymes (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 36: |
Line 37: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43504]] | |
| - | [[Category: Large Structures]] | |
| - | [[Category: Bueno, M]] | |
| - | [[Category: Cremades, N]] | |
| - | [[Category: Hermoso, J A]] | |
| - | [[Category: Martinez-Julvez, M]] | |
| - | [[Category: Perez-Dorado, I]] | |
| - | [[Category: Sancho, J]] | |
| - | [[Category: Electron transport]] | |
| - | [[Category: Flavoprotein]] | |
| - | [[Category: Fmn]] | |
| | [[Category: Helicobacter pylori]] | | [[Category: Helicobacter pylori]] |
| - | [[Category: Transport protein]] | + | [[Category: Large Structures]] |
| | + | [[Category: Bueno M]] |
| | + | [[Category: Cremades N]] |
| | + | [[Category: Hermoso JA]] |
| | + | [[Category: Martinez-Julvez M]] |
| | + | [[Category: Perez-Dorado I]] |
| | + | [[Category: Sancho J]] |
| Structural highlights
Function
FLAV_HELPY Low-potential electron donor to a number of redox enzymes (By similarity).
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
Flavodoxins, noncovalent complexes between apoflavodoxins and flavin mononucleotide (FMN), are useful models to investigate the mechanism of protein/flavin recognition. In this respect, the only available crystal structure of an apoflavodoxin (that from Anabaena) showed a closed isoalloxazine pocket and the presence of a bound phosphate ion, which posed many questions on the recognition mechanism and on the potential physiological role exerted by phosphate ions. To address these issues we report here the X-ray structure of the apoflavodoxin from the pathogen Helicobacter pylori. The protein naturally lacks one of the conserved aromatic residues that close the isoalloxazine pocket in Anabaena, and the structure has been determined in a medium lacking phosphate. In spite of these significant differences, the isoallozaxine pocket in H. pylori apoflavodoxin appears also closed and a chloride ion is bound at a native-like FMN phosphate site. It seems thus that it is a general characteristic of apoflavodoxins to display closed, non-native, isoalloxazine binding sites together with native-like, rather promiscuous, phosphate binding sites that can bear other available small anions present in solution. In this respect, both binding energy hot spots of the apoflavodoxin/FMN complex are initially unavailable to FMN binding and the specific spot for FMN recognition may depend on the dynamics of the two candidate regions. Molecular dynamics simulations show that the isoalloxazine binding loops are intrinsically flexible at physiological temperatures, thus facilitating the intercalation of the cofactor, and that their mobility is modulated by the anion bound at the phosphate site.
Common conformational changes in flavodoxins induced by FMN and anion binding: the structure of Helicobacter pylori apoflavodoxin.,Martinez-Julvez M, Cremades N, Bueno M, Perez-Dorado I, Maya C, Cuesta-Lopez S, Prada D, Falo F, Hermoso JA, Sancho J Proteins. 2007 Nov 15;69(3):581-94. PMID:17623845[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Martinez-Julvez M, Cremades N, Bueno M, Perez-Dorado I, Maya C, Cuesta-Lopez S, Prada D, Falo F, Hermoso JA, Sancho J. Common conformational changes in flavodoxins induced by FMN and anion binding: the structure of Helicobacter pylori apoflavodoxin. Proteins. 2007 Nov 15;69(3):581-94. PMID:17623845 doi:10.1002/prot.21410
|
