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==Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli== | ==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=''> | <StructureSection load='3fwl' size='340' side='right' caption='[[3fwl]], [[Resolution|resolution]] 3.09Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fwm|3fwm]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fwm|3fwm]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0149, JW0145, mrcB, pbpF, ponB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0149, JW0145, mrcB, pbpF, ponB ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fwl OCA], [http://pdbe.org/3fwl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fwl RCSB], [http://www.ebi.ac.uk/pdbsum/3fwl PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fwl OCA], [http://pdbe.org/3fwl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fwl RCSB], [http://www.ebi.ac.uk/pdbsum/3fwl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fwl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3fwl" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3fwl" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:51, 1 November 2017
Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coliCrystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli
Structural highlights
Function[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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDrug-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Bacillus coli migula 1895
- 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