3b44
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:3b44.jpg|left|200px]] | [[Image:3b44.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_3b44", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_3b44| PDB=3b44 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal structure of GlpG W136A mutant''' | '''Crystal structure of GlpG W136A mutant''' | ||
| Line 29: | Line 26: | ||
[[Category: Maegawa, S.]] | [[Category: Maegawa, S.]] | ||
[[Category: Wang, Y.]] | [[Category: Wang, Y.]] | ||
| - | [[Category: | + | [[Category: Dna-binding]] |
| - | [[Category: | + | [[Category: Glycerol metabolism]] |
| - | [[Category: | + | [[Category: Inner membrane]] |
| - | [[Category: | + | [[Category: Integral membrane protein]] |
| - | [[Category: | + | [[Category: Intramembrane protease]] |
| - | [[Category: | + | [[Category: Serine protease]] |
| - | [[Category: | + | [[Category: Transmembrane]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:22:27 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:22, 4 May 2008
Crystal structure of GlpG W136A mutant
Overview
Intramembrane proteases are important enzymes in biology. The recently solved crystal structures of rhomboid protease GlpG have provided useful insights into the mechanism of these membrane proteins. Besides revealing an internal water-filled cavity that harbored the Ser-His catalytic dyad, the crystal structure identified a novel structural domain (L1 loop) that lies on the side of the transmembrane helices. Here, using site-directed mutagenesis, we confirmed that the L1 loop is partially embedded in the membrane, and showed that alanine substitution of a highly preferred tryptophan (Trp136) at the distal tip of the L1 loop near the lipid:water interface reduced GlpG proteolytic activity. Crystallographic analysis showed that W136A mutation did not modify the structure of the protease. Instead, the polarity for a small and lipid-exposed protein surface at the site of the mutation has changed. The crystal structure, now refined at 1.7 A resolution, also clearly defined a 20-A-wide hydrophobic belt around the protease, which likely corresponded to the thickness of the compressed membrane bilayer around the protein. This improved structural model predicts that all critical elements of the catalysis, including the catalytic serine and the L5 cap, need to be positioned within a few angstroms of the membrane surface, and may explain why the protease activity is sensitive to changes in the protein:lipid interaction. Based on these findings, we propose a model where the end of the substrate transmembrane helix first partitions out of the hydrophobic core region of the membrane before it bends into the protease active site for cleavage.
About this Structure
3B44 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG., Wang Y, Maegawa S, Akiyama Y, Ha Y, J Mol Biol. 2007 Dec 7;374(4):1104-13. Epub 2007 Oct 11. PMID:17976648 Page seeded by OCA on Sun May 4 20:22:27 2008
