2ae0
From Proteopedia
(New page: 200px<br /><applet load="2ae0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ae0, resolution 2.000Å" /> '''Crystal structure o...) |
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| - | [[Image:2ae0.gif|left|200px]]<br /><applet load="2ae0" size=" | + | [[Image:2ae0.gif|left|200px]]<br /><applet load="2ae0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ae0, resolution 2.000Å" /> | caption="2ae0, resolution 2.000Å" /> | ||
'''Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold'''<br /> | '''Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Lytic transglycosylases are bacterial enzymes involved in the maintenance | + | 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== | ==About this Structure== | ||
| - | 2AE0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with EDO and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2AE0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AE0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dijkstra, B | + | [[Category: Dijkstra, B W.]] |
| - | [[Category: Straaten, K | + | [[Category: Straaten, K E.Van.]] |
| - | [[Category: Thunnissen, A | + | [[Category: Thunnissen, A M.W H.]] |
[[Category: Vollmer, W.]] | [[Category: Vollmer, W.]] | ||
[[Category: ACY]] | [[Category: ACY]] | ||
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[[Category: small mixed parallel/antiparallel six stranded beta barrel]] | [[Category: small mixed parallel/antiparallel six stranded beta barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:26:25 2008'' |
Revision as of 14:26, 21 February 2008
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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 with and as ligands. 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
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