2F2B: Crystal Structure Of Integral Membrane Protein Aquaporin Aqpm At 1.68a Resolution

Citation:
Abstract
To explore the structural basis of the unique selectivity spectrum and conductance of the transmembrane channel protein AqpM from the archaeon Methanothermobacter marburgensis, we determined the structure of AqpM to 1.68-A resolution by x-ray crystallography. The structure establishes AqpM as being in a unique subdivision between the two major subdivisions of aquaporins, the water-selective aquaporins, and the water-plus-glycerol-conducting aquaglyceroporins. In AqpM, isoleucine replaces a key histidine residue found in the lumen of water channels, which becomes a glycine residue in aquaglyceroporins. As a result of this and other side-chain substituents in the walls of the channel, the channel is intermediate in size and exhibits differentially tuned electrostatics when compared with the other subfamilies.
PDB ID: 2F2BDownload
MMDB ID: 36523
PDB Deposition Date: 2005/11/15
Updated in MMDB: 2005/12
Experimental Method:
x-ray diffraction
Resolution: 1.68  Å
Source Organism:
Similar Structures:
Biological Unit for 2F2B: tetrameric; determined by author and by software (PISA,PQS)
Molecular Components in 2F2B
Label Count Molecule
Proteins (4 molecules)
4
Aquaporin Aqpm(Gene symbol: MTBMA_RS02725)
Molecule annotation
Chemicals (4 molecules)
1
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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