PDBsum entry 2wc1

Electron transport

PDB id: 2wc1

Contents

Protein chain

182 a.a. *

Ligands

FMN

Waters ×74

* Residue conservation analysis

PDB id:

2wc1

Name:

Electron transport

Title:

Three-dimensional structure of the nitrogen fixation flavodoxin (niff) from rhodobacter capsulatus at 2.2 a

Structure:

Flavodoxin. Chain: a. Engineered: yes

Source:

Rhodobacter capsulatus. Organism_taxid: 1061. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

2.17Å R-factor: 0.246 R-free: 0.267

Authors:

I.Perez-Dorado,C.Bittel,J.A.Hermoso,N.Cortez,N.Carrillo

Key ref:

I.Pérez-Dorado et al. (2013). Structural and phylogenetic analysis of Rhodobacter capsulatus NifF: uncovering general features of nitrogen-fixation (nif)-flavodoxins. Int J Mol Sci, 14, 1152-1163. PubMed id: 23303276

Date:

06-Mar-09 Release date: 21-Apr-10

Protein chain

P52967  (FLAV_RHOCB) -  Flavodoxin from Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)

Seq: 182 a.a.

Struc: 182 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Int J Mol Sci 14:1152-1163 (2013)

PubMed id: 23303276

Structural and phylogenetic analysis of Rhodobacter capsulatus NifF: uncovering general features of nitrogen-fixation (nif)-flavodoxins.

I.Pérez-Dorado, A.Bortolotti, N.Cortez, J.A.Hermoso.

ABSTRACT

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.