2wc1

From Proteopedia

(Difference between revisions)

Revision as of 11:03, 6 April 2022

Three-dimensional Structure of the Nitrogen Fixation Flavodoxin (NifF) from Rhodobacter capsulatus at 2.2 A

Structural highlights

2wc1 is a 1 chain structure with sequence from "rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907. 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

[FLAV_RHOCB] Low-potential electron donor to a number of redox enzymes. NifF is the electron donor to nitrogenase.

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

Analysis of the crystal structure of NifF from Rhodobacter capsulatus and its homologues reported so far reflects the existence of unique structural features in nif flavodoxins: a leucine at the re face of the isoalloxazine, an eight-residue insertion at the C-terminus of the 50's loop and a remarkable difference in the electrostatic potential surface with respect to non-nif flavodoxins. A phylogenetic study on 64 sequences from 52 bacterial species revealed four clusters, including different functional prototypes, correlating the previously defined as "short-chain" with the firmicutes flavodoxins and the "long-chain" with gram-negative species. The comparison of Rhodobacter NifF structure with other bacterial flavodoxin prototypes discloses the concurrence of specific features of these functional electron donors to nitrogenase.

Structural and Phylogenetic Analysis of Rhodobacter capsulatus NifF: Uncovering General Features of Nitrogen-fixation (nif)-Flavodoxins.,Perez-Dorado I, Bortolotti A, Cortez N, Hermoso JA Int J Mol Sci. 2013 Jan 9;14(1):1152-63. doi: 10.3390/ijms14011152. PMID:23303276^[1]

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

References

↑ Perez-Dorado I, Bortolotti A, Cortez N, Hermoso JA. Structural and Phylogenetic Analysis of Rhodobacter capsulatus NifF: Uncovering General Features of Nitrogen-fixation (nif)-Flavodoxins. Int J Mol Sci. 2013 Jan 9;14(1):1152-63. doi: 10.3390/ijms14011152. PMID:23303276 doi:http://dx.doi.org/10.3390/ijms14011152

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/2wc1"

@@ Line 3: / Line 3: @@
 <StructureSection load='2wc1' size='340' side='right'caption='[[2wc1]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wc1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WC1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WC1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wc1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WC1 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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://proteopedia.org/fgij/fg.htm?mol=2wc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wc1 OCA], [http://pdbe.org/2wc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wc1 RCSB], [http://www.ebi.ac.uk/pdbsum/2wc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wc1 ProSAT]</span></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=2wc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wc1 OCA], [https://pdbe.org/2wc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wc1 RCSB], [https://www.ebi.ac.uk/pdbsum/2wc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wc1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FLAV_RHOCB FLAV_RHOCB]] Low-potential electron donor to a number of redox enzymes. NifF is the electron donor to nitrogenase.
+[[https://www.uniprot.org/uniprot/FLAV_RHOCB FLAV_RHOCB]] Low-potential electron donor to a number of redox enzymes. NifF is the electron donor to nitrogenase.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2wc1

From Proteopedia

Revision as of 11:03, 6 April 2022

Three-dimensional Structure of the Nitrogen Fixation Flavodoxin (NifF) from Rhodobacter capsulatus at 2.2 A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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