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3fwl
From Proteopedia
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| - | [[Image:3fwl.png|left|200px]] | ||
| - | + | ==Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli== | |
| + | <StructureSection load='3fwl' size='340' side='right'caption='[[3fwl]], [[Resolution|resolution]] 3.09Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3fwl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FWL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M0E:MOENOMYCIN'>M0E</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fwm|3fwm]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0149, JW0145, mrcB, pbpF, ponB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=3fwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fwl OCA], [https://pdbe.org/3fwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fwl RCSB], [https://www.ebi.ac.uk/pdbsum/3fwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fwl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/PBPB_ECOLI PBPB_ECOLI]] Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). | ||
| + | == 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/fw/3fwl_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3fwl ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Drug-resistant bacteria have caused serious medical problems in recent years, and the need for new antibacterial agents is undisputed. Transglycosylase, a multidomain membrane protein essential for cell wall synthesis, is an excellent target for the development of new antibiotics. Here, we determined the X-ray crystal structure of the bifunctional transglycosylase penicillin-binding protein 1b (PBP1b) from Escherichia coli in complex with its inhibitor moenomycin to 2.16-A resolution. In addition to the transglycosylase and transpeptidase domains, our structure provides a complete visualization of this important antibacterial target, and reveals a domain for protein-protein interaction and a transmembrane helix domain essential for substrate binding, enzymatic activity, and membrane orientation. | ||
| - | + | Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli.,Sung MT, Lai YT, Huang CY, Chou LY, Shih HW, Cheng WC, Wong CH, Ma C Proc Natl Acad Sci U S A. 2009 May 19. PMID:19458048<ref>PMID:19458048</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3fwl" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Penicillin-binding protein|Penicillin-binding protein]] | + | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Chou, L Y | + | [[Category: Bacillus coli migula 1895]] |
| - | [[Category: Huang, C Y | + | [[Category: Large Structures]] |
| - | [[Category: Lai, Y T | + | [[Category: Chou, L Y]] |
| - | [[Category: Ma, C | + | [[Category: Huang, C Y]] |
| - | [[Category: Sung, M T | + | [[Category: Lai, Y T]] |
| - | [[Category: Wong, C H | + | [[Category: Ma, C]] |
| + | [[Category: Sung, M T]] | ||
| + | [[Category: Wong, C H]] | ||
[[Category: Alternative initiation]] | [[Category: Alternative initiation]] | ||
[[Category: Antibiotic resistance]] | [[Category: Antibiotic resistance]] | ||
Current revision
Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli
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Categories: Bacillus coli migula 1895 | Large Structures | Chou, L Y | Huang, C Y | Lai, Y T | Ma, C | Sung, M T | Wong, C H | Alternative initiation | Antibiotic resistance | Antibiotics design | Bacterial cell wall synthesis | Cell inner membrane | Cell membrane | Cell shape | Cell wall biogenesis/degradation | Glycosyltransferase | Hydrolase | Membrane | Multifunctional enzyme | Penicillin-binding protein | Peptidoglycan synthesis | Signal-anchor | Transferase | Transmembrane

