This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1mal

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mal OCA], [http://www.ebi.ac.uk/pdbsum/1mal PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mal RCSB]</span>
}}
}}
Line 25: Line 28:
[[Category: outer membrane protein]]
[[Category: outer membrane protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:41:05 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:13:40 2008''

Revision as of 19:13, 30 March 2008


PDB ID 1mal

Drag the structure with the mouse to rotate
, resolution 3.10Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURAL BASIS FOR SUGAR TRANSLOCATION THROUGH MALTOPORIN CHANNELS AT 3.1 ANGSTROMS RESOLUTION


Overview

Trimeric maltoporin (LamB protein) facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The crystal structure of maltoporin from Escherichia coli, determined to a resolution of 3.1 angstroms, reveals an 18-stranded, antiparallel beta-barrel that forms the framework of the channel. Three inwardly folded loops contribute to a constriction about halfway through the channel. Six contingent aromatic residues line the channel and form a path from the vestibule to the periplasmic outlet. Soaking of a crystal with maltotriose revealed binding of the sugar to this hydrophobic track across the constriction, which suggests that maltose and linear oligosaccharides may be translocated across the membrane by guided diffusion along this path.

About this Structure

1MAL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution., Schirmer T, Keller TA, Wang YF, Rosenbusch JP, Science. 1995 Jan 27;267(5197):512-4. PMID:7824948

Page seeded by OCA on Sun Mar 30 22:13:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools