2ae0
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2ae0 |SIZE=350|CAPTION= <scene name='initialview01'>2ae0</scene>, resolution 2.000Å | |PDB= 2ae0 |SIZE=350|CAPTION= <scene name='initialview01'>2ae0</scene>, resolution 2.000Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= mlta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= mlta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK11162 mltA], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam03562 MltA], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam06725 3D]</span> | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ae0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ae0 OCA], [http://www.ebi.ac.uk/pdbsum/2ae0 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2ae0 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 28: | ||
[[Category: Thunnissen, A M.W H.]] | [[Category: Thunnissen, A M.W H.]] | ||
[[Category: Vollmer, W.]] | [[Category: Vollmer, W.]] | ||
| - | [[Category: ACY]] | ||
| - | [[Category: EDO]] | ||
[[Category: double-psi beta-barrel]] | [[Category: double-psi beta-barrel]] | ||
[[Category: helical sub-domain]] | [[Category: helical sub-domain]] | ||
[[Category: small mixed parallel/antiparallel six stranded beta barrel]] | [[Category: small mixed parallel/antiparallel six stranded beta barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:20:02 2008'' |
Revision as of 04:20, 26 March 2008
| |||||||
| , resolution 2.000Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | mlta (Escherichia coli) | ||||||
| Domains: | mltA, MltA, 3D | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Wed Mar 26 06:20:02 2008
