2ae0

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(New page: 200px<br /><applet load="2ae0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ae0, resolution 2.000&Aring;" /> '''Crystal structure o...)
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[[Image:2ae0.gif|left|200px]]<br /><applet load="2ae0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ae0, resolution 2.000&Aring;" />
 
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'''Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold'''<br />
 
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==Overview==
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==Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold==
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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.
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<StructureSection load='2ae0' size='340' side='right'caption='[[2ae0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2ae0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AE0 FirstGlance]. <br>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AE0 OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ae0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ae0 OCA], [https://pdbe.org/2ae0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ae0 RCSB], [https://www.ebi.ac.uk/pdbsum/2ae0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ae0 ProSAT]</span></td></tr>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16139297 16139297]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MLTA_ECOLI MLTA_ECOLI] Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Degrades murein glycan strands and insoluble, high-molecular weight murein sacculi.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/2ae0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ae0 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Dijkstra BW]]
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[[Category: Straaten, K.E.Van.]]
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[[Category: Thunnissen AMWH]]
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[[Category: Thunnissen, A.M.W.H.]]
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[[Category: Van Straaten KE]]
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[[Category: Vollmer, W.]]
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[[Category: Vollmer W]]
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[[Category: ACY]]
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[[Category: EDO]]
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[[Category: double-psi beta-barrel]]
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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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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:04:11 2007''
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Current revision

Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold

PDB ID 2ae0

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