1NQF: Outer Membrane Cobalamin Transporter (btub) From E. Coli, Methionine Substiution Construct For Se-met Sad Phasing

Citation:
Abstract
The outer membranes of Gram-negative bacteria possess transport proteins essential for uptake of scarce nutrients. In TonB-dependent transporters, a conserved sequence of seven residues, the Ton box, faces the periplasm and interacts with the inner membrane TonB protein to energize an active transport cycle. A critical mechanistic step is the structural change in the Ton box of the transporter upon substrate binding; this essential transmembrane signaling event increases the affinity of the transporter for TonB and enables active transport to proceed. We have solved crystal structures of BtuB, the outer membrane cobalamin transporter from Escherichia coli, in the absence and presence of cyanocobalamin (vitamin B(12)). In these structures, the Ton box is ordered and undergoes a conformational change in the presence of bound substrate. Calcium has been implicated as a necessary factor for the high-affinity binding (K(d) approximately 0.3 nM) of cyanocobalamin to BtuB. We observe two bound calcium ions that order three extracellular loops of BtuB, thus providing a direct (and unusual) structural role for calcium.
PDB ID: 1NQFDownload
MMDB ID: 22717
PDB Deposition Date: 2003/1/21
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 1NQF: monomeric; determined by author
Molecular Components in 1NQF
Label Count Molecule
Protein (1 molecule)
1
Vitamin B12 Receptor(Gene symbol: btuB)
Molecule annotation
Chemicals (7 molecules)
1
1
2
6
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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