3vma
From Proteopedia
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| - | [[ | + | ==Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli== |
| + | <StructureSection load='3vma' size='340' side='right' caption='[[3vma]], [[Resolution|resolution]] 2.16Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3vma]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3fwm 3fwm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VMA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VMA FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M0E:MOENOMYCIN'>M0E</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fwl|3fwl]]</td></tr> | ||
| + | <tr><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 Escherichia coli])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vma OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vma RCSB], [http://www.ebi.ac.uk/pdbsum/3vma PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <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> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Penicillin-binding protein|Penicillin-binding protein]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Cheng, W C.]] | [[Category: Cheng, W C.]] | ||
Revision as of 07:37, 5 June 2014
Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli
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