1d0l

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[[Image:1d0l.jpg|left|200px]]
 
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{{Structure
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==THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35 IN COMPLEX WITH BULGECIN A==
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|PDB= 1d0l |SIZE=350|CAPTION= <scene name='initialview01'>1d0l</scene>, resolution 1.97&Aring;
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<StructureSection load='1d0l' size='340' side='right'caption='[[1d0l]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BLG:4-O-(4-O-SULFONYL-N-ACETYLGLUCOSAMININYL)-5-METHYLHYDROXY-L-PROLINE-TAURINE'>BLG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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<table><tr><td colspan='2'>[[1d0l]] 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=1D0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D0L FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.97&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLG:4-O-(4-O-SULFONYL-N-ACETYLGLUCOSAMININYL)-5-METHYLHYDROXY-L-PROLINE-TAURINE'>BLG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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|DOMAIN=
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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=1d0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d0l OCA], [https://pdbe.org/1d0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d0l RCSB], [https://www.ebi.ac.uk/pdbsum/1d0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d0l ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1qus|1QUS]], [[1qut|1QUT]], [[1qdr|1QDR]], [[1qdt|1QDT]], [[1d0k|1D0K]], [[1d0l|1D0L]], [[1d0m|1D0M]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d0l OCA], [http://www.ebi.ac.uk/pdbsum/1d0l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d0l RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/MLTB_ECOLI MLTB_ECOLI] Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division.
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== Evolutionary Conservation ==
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'''THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35 IN COMPLEX WITH BULGECIN A'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d0/1d0l_consurf.spt"</scriptWhenChecked>
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Lytic transglycosylases catalyze the cleavage of the beta-1, 4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan with concomitant formation of a 1,6-anhydro bond in the MurNAc residue. To understand the reaction mechanism of Escherichia coli lytic transglycosylase Slt35, three crystal structures have been determined of Slt35 in complex with two different peptidoglycan fragments and with the lytic transglycosylase inhibitor bulgecin A. The complexes define four sugar-binding subsites (-2, -1, +1, and +2) and two peptide-binding sites in a large cleft close to Glu162. The Glu162 side chain is between the -1 and +1 sugar-binding sites, in agreement with a function as catalytic acid/base. The complexes suggest additional contributions to catalysis from Ser216 and Asn339, residues which are conserved among the MltB/Slt35 lytic transglycosylases.
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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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==About this Structure==
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</jmolCheckbox>
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1D0L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D0L OCA].
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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=1d0l ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan., van Asselt EJ, Kalk KH, Dijkstra BW, Biochemistry. 2000 Feb 29;39(8):1924-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10684641 10684641]
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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: Asselt, E J.van.]]
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[[Category: Dijkstra BW]]
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[[Category: Dijkstra, B W.]]
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[[Category: Kalk KH]]
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[[Category: Kalk, K H.]]
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[[Category: Van Asselt EJ]]
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[[Category: alpha-helical protein with a five stranded anti-parallel beta-sheet]]
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[[Category: ef-hand]]
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[[Category: glycosyl transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:32:08 2008''
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Current revision

THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35 IN COMPLEX WITH BULGECIN A

PDB ID 1d0l

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