2ae0
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2ae0.gif|left|200px]] | [[Image:2ae0.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2ae0", 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_2ae0| PDB=2ae0 | SCENE= }} | |
| - | | | + | |
| - | | | + | |
| - | }} | + | |
'''Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold''' | '''Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold''' | ||
| Line 29: | Line 26: | ||
[[Category: Thunnissen, A M.W H.]] | [[Category: Thunnissen, A M.W H.]] | ||
[[Category: Vollmer, W.]] | [[Category: Vollmer, W.]] | ||
| - | [[Category: | + | [[Category: Double-psi beta-barrel]] |
| - | [[Category: | + | [[Category: Helical sub-domain]] |
| - | [[Category: | + | [[Category: Small mixed parallel/antiparallel six stranded beta barrel]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:55:39 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:55, 3 May 2008
Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold
Overview
Lytic transglycosylases are bacterial enzymes involved in the maintenance and growth of the bacterial cell-wall peptidoglycan. They cleave the beta-(1,4)-glycosidic bonds in peptidoglycan forming non-reducing 1,6-anhydromuropeptides. The crystal structure of the lytic transglycosylase MltA from Escherichia coli without a membrane anchor was solved at 2.0A resolution. The enzyme has a fold completely different from those of the other known lytic transglycosylases. It contains two domains, the largest of which has a double-psi beta-barrel fold, similar to that of endoglucanase V from Humicola insolens. The smaller domain also has a beta-barrel fold topology, which is weakly related to that of the RNA-binding domain of ribosomal proteins L25 and TL5. A large groove separates the two domains, which can accommodate a glycan strand, as shown by molecular modelling. Several conserved residues, one of which is in a position equivalent to that of the catalytic acid of the H.insolens endoglucanase, flank this putative substrate-binding groove. Mutation of this residue, Asp308, abolished all activity of the enzyme, supporting the direct participation of this residue in catalysis.
About this Structure
2AE0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold., van Straaten KE, Dijkstra BW, Vollmer W, Thunnissen AM, J Mol Biol. 2005 Oct 7;352(5):1068-80. PMID:16139297 Page seeded by OCA on Sat May 3 18:55:39 2008
