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2ae0

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[[Image:2ae0.gif|left|200px]]
[[Image:2ae0.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2ae0", creates the "Structure Box" on the page.
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|GENE= mlta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|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>
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{{STRUCTURE_2ae0| PDB=2ae0 | SCENE= }}
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|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.rcsb.org/pdb/explore.do?structureId=2ae0 RCSB]</span>
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'''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'''
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[[Category: Thunnissen, A M.W H.]]
[[Category: Thunnissen, A M.W H.]]
[[Category: Vollmer, W.]]
[[Category: Vollmer, W.]]
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[[Category: double-psi beta-barrel]]
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[[Category: Double-psi beta-barrel]]
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[[Category: helical sub-domain]]
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[[Category: Helical sub-domain]]
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[[Category: small mixed parallel/antiparallel six stranded beta barrel]]
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[[Category: Small mixed parallel/antiparallel six stranded beta barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:55:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:51:19 2008''
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Revision as of 15:55, 3 May 2008

Template:STRUCTURE 2ae0

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

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