2pi8: Difference between revisions

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-[[Image:2pi8.jpg|left|200px]]<br /><applet load="2pi8" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2pi8, resolution 2.250&Aring;" />
-'''Crystal structure of E. coli MltA with bound chitohexaose'''<br />
-==Overview==
+==Crystal structure of E. coli MltA with bound chitohexaose==
-Crystal structures of an inactive mutant (D308A) of the lytic, transglycosylase MltA from Escherichia coli have been determined in two, different apo-forms, as well as in complex with the substrate analogue, chitohexaose. The chitohexaose binds with all six saccharide residues in, the active site groove, with an intact glycosidic bond at the bond, cleavage center. Its binding induces a large reorientation of the two, structural domains in MltA, narrowing the active site groove and allowing, tight interactions of the oligosaccharide with residues from both domains., The structures identify residues in MltA with key roles in the binding and, recognition of peptidoglycan and confirm that Asp-308 is the single, catalytic residue, acting as a general acid/base. Moreover, the structures, suggest that catalysis involves a high energy conformation of the scissile, glycosidic linkage and that the putative oxocarbenium ion intermediate is, stabilized by the dipole moment of a nearby alpha-helix.
+<StructureSection load='2pi8' size='340' side='right'caption='[[2pi8]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2pi8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PI8 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pi8 OCA], [https://pdbe.org/2pi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pi8 RCSB], [https://www.ebi.ac.uk/pdbsum/2pi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pi8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pi/2pi8_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2pi8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Crystal structures of an inactive mutant (D308A) of the lytic transglycosylase MltA from Escherichia coli have been determined in two different apo-forms, as well as in complex with the substrate analogue chitohexaose. The chitohexaose binds with all six saccharide residues in the active site groove, with an intact glycosidic bond at the bond cleavage center. Its binding induces a large reorientation of the two structural domains in MltA, narrowing the active site groove and allowing tight interactions of the oligosaccharide with residues from both domains. The structures identify residues in MltA with key roles in the binding and recognition of peptidoglycan and confirm that Asp-308 is the single catalytic residue, acting as a general acid/base. Moreover, the structures suggest that catalysis involves a high energy conformation of the scissile glycosidic linkage and that the putative oxocarbenium ion intermediate is stabilized by the dipole moment of a nearby alpha-helix.
-==About this Structure==
+Structure of Escherichia coli Lytic transglycosylase MltA with bound chitohexaose: implications for peptidoglycan binding and cleavage.,van Straaten KE, Barends TR, Dijkstra BW, Thunnissen AM J Biol Chem. 2007 Jul 20;282(29):21197-205. Epub 2007 May 14. PMID:17502382<ref>PMID:17502382</ref>
-PI8 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 PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PI8 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Structure of Escherichia coli Lytic transglycosylase MltA with bound chitohexaose: implications for peptidoglycan binding and cleavage., van Straaten KE, Barends TR, Dijkstra BW, Thunnissen AM, J Biol Chem. 2007 Jul 20;282(29):21197-205. Epub 2007 May 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17502382 17502382]
+</div>
-[[Category: Escherichia coli]]
+<div class="pdbe-citations 2pi8" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+== References ==
-[[Category: Barends, T.R.M.]]
+<references/>
-[[Category: Dijkstra, B.W.]]
+__TOC__
-[[Category: Straaten, K.E.van.]]
+</StructureSection>
-[[Category: Thunnissen, A.M.W.H.]]
+[[Category: Escherichia coli K-12]]
-[[Category: PO4]]
+[[Category: Large Structures]]
-[[Category: double-psi beta-barrel; protein-sugar complex; lytic transglycosylase]]
+[[Category: Barends TRM]]
+[[Category: Dijkstra BW]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:32:49 2007''
+[[Category: Thunnissen AMWH]]
+[[Category: Van Straaten KE]]